Search

Your search keyword '"Welfle, Heinz"' showing total 88 results
Start Over Author "Welfle, Heinz"
88 results on '"Welfle, Heinz"'

55. The Influence of Mn2+ on DNA structure in the presence of Na+ ions: A Raman spectroscopic study.

Author

Muntean, Cristina M., Misselwitz, Rolf, and Welfle, Heinz

Subjects
RAMAN spectroscopy, MANGANESE, SODIUM ions, DNA, ADENINE, RAMAN effect
Abstract

The influence of Mn2+ ions on the structure of natural calf thymus DNA was studied by Raman spectroscopy. Measurements were done at room temperature and pH 6.2±0.2, in the presence of the physiological concentration of 150 mM Na+ ions, and in the presence of Mn2+ concentrations that varied between 0 and 600 mM. No condensation of DNA was observed at any of the Mn2+ concentrations. At 5 mM Mn2+ and 150 mM Na+ no significant influence of Mn2+ ions on the DNA structure can be observed. Compared with our previous results obtained at 10 mM Na+ ions, binding of Mn2+ ions to charged phosphate groups and to DNA bases is inhibited in the presence of 150 mM Na+ ions. DNA backbone conformational changes were not observed in the whole concentration range of Mn2+ ions as judging from the Raman spectra. No evidence for DNA melting was identified. A high Mn2+ affinity for binding to guanine N7 and possibly, in a much lesser extent, to adenine have been found. [ABSTRACT FROM AUTHOR]

Published
2006
Full Text
View/download PDF

56. Mn2+–DNA interactions in aqueous systems: A Raman spectroscopic study.

Author

Muntean, Cristina M., Misselwitz, Rolf, Dostál, Lubomir, and Welfle, Heinz

Subjects
RAMAN spectroscopy, SPECTRUM analysis, DNA, NUCLEIC acids, MOLECULAR spectra, GENES
Abstract

Interaction of natural calf thymus DNA with Mn2+ ions was studied by means of Raman spectroscopy. Spectra of DNA in 10 mM Na-cacodylate buffer, pH 6.2, 10 mM NaCl and in buffer containing Mn2+ ions were measured at room temperature. Mn2+ concentrations varied between 0 and 0.6 M. DNA backbone conformational changes and DNA denaturation were not observed in the concentration range 0 and 0.5 M, however, DNA condensation was observed at a critical concentration of 100 mM Mn2+ that prevented the measurement of Raman spectra. Binding of Mn2+ to the charged phosphate groups of DNA is indicated in the spectra. A high affinity of Mn2+ for guanine N7 was obvious, and binding to adenine was barely suggested. [ABSTRACT FROM AUTHOR]

Published
2006
Full Text
View/download PDF

59. Conformations and conformational changes of four Phe→Trp variants of the DNA-binding histone-like protein, HBsu, from Bacillus subtilis studied by circular dichroism and fluorescence spectroscopy.

Author

Welfle, Heinz, Misselwitz, Rolf, Welfle, Karin, Schindelin, Hermann, Scholtz, Andreas S., and Heinemann, Udo

Subjects
*BACILLUS subtilis, *DNA-binding proteins, *HISTONES, *GENETIC mutation, *DICHROISM, *FLUORESCENCE spectroscopy
Abstract

Circular dichroic spectra in the region 180-260 nm of the DNA-binding histone-like protein. HBsu, from Bacillus subtillis and of four mutants with a Phe residue replaced by Trp, i.e. [F29W]HBsu, [F47W]HBsu, [F50W]HBsu and [F79W]HBsu, show minor differences only and demonstrate the general similarity of the conformations of these proteins. Fluorescence maxima at 315-320 nm and 330-335 nm indicate a more hydrophobic environment or a more effective stacking of Trp residues in mutants [F29W]HBsu and [F50W]HBsu in comparison to [F47W]HBsu and [F79W]HBsu, respectively. Unfolding of the mutants in high-ionic-strength buffers by increasing concentrations of urea results in a red shift of the fluorescence emission maxima to about 350 nm: the fluorescence intensities decrease strongly for [F29W]HBsu and [F50W]HBsu but show a small increase for [F47W]HBsu and [F79W]HBsu. The data suggest complex unfolding patterns with subtle differences between the single mutants. The circular dichoir spectra in the region 250-320 nm are dominated by the effects of the Trp residues and signal position-dependent differences in the environment of the Trp residues. The conformation of the mutant proteins depend on the ionic strength of the buffer and become more stable against unfolding by denaturants or increasing temperatures at higher ionic strength. At low ionic strength a pronounced protein-concentration dependence of the conformation of the mutants is seen. [ABSTRACT FROM AUTHOR]

Published
1993
Full Text
View/download PDF

60. Salt-dependent and protein-concentration-dependent changes in the solution structure of the DNA-=binding histone-like protein, HBsu, from <em>Bacillus subtilis</em>.

Author

Welfle, Heinz, Misselwitz, Rolf, Welfle, Karin, Groch, Nicolas, and Heinemann, Udo

Subjects
*DNA-binding proteins, *PROTEINS, *BACILLUS subtilis, *BACILLUS (Bacteria), *BACTERIAL proteins, *CIRCULAR dichroism, *CARRIER proteins
Abstract

The solution structure of the histone-like DNA-binding protein, HBsu, from Bacillus subtilis in 2 mM sodium cacodylate, pH 7.5, is sensitive to the ionic strength of the buffer. This was shown by circular dichroism measurements at different concentrations of sodium chloride and potassium fluoride. The stability of HBsu is also influenced; at HBsu concentrations of about 0.1 mg · ml-1, melting temperatures of 32°C and 55°C were found in the absence of potassium fluoride and in the presence of 0.5 M potassium fluoride, respectively, exhibiting drastic ionic-strength-dependent differences in the temperature-induced unfolding of HBsu. Furthermore, at low ionic strength, circular dichroism spectra vary markedly depending on the HBsu concentration in the approximate range 0.2-3 mg · ml-1. Such protein-concentration dependent differences in the spectra were not observed in the presence of 0.5 M potassium fluoride. Very similar circular dichroism spectra of HBsu and the histone-like DNA-binding protein of Bacillus stearothermophilus (HBst) at high ionic strength, indicate comparable structures of both proteins under these conditions. Estimation of the secondary structure content from the circular dichroism spectra yields data which are in satisfactory agreement with the values obtained from the crystal structure of HBst. Transition temperatures of 45°C and 61 °C were found in differential scanning calorimetric measurements performed with HBsu in potassium-fluoride-free buffer and in the presence of 0.5 M potassium fluoride, respectively. The thermodynamic data point to the melting of native HBsu dimers into two denatured monomers. [ABSTRACT FROM AUTHOR]

Published
1992
Full Text
View/download PDF

63. A-form to A'-form conformational switch of double helices in rat liver 5S and 5.8S rRNA.

Author

Müller, Jürgen Joachim, Misselwitz, Rolf, Zirwer, Dietrich, Damaschun, Gregor, and Welfle, Heinz

Subjects
X-ray scattering, MOLECULES, RNA-protein interactions, HYDROCHLORIC acid, LIVER, LABORATORY rats
Abstract

The wide-angle X-ray scattering of rat liver 5S rRNA and 5.8S rRNA molecules showed significant differences in the positions of the scattering maxima when dissolved in Mg2+-containing Tris/HCl buffer or in Mg2+-depleted buffer. A comparison of the experimental curves with theoretical curves calculated from atomic coordinates of double-helical models proved a switch from A form to A′ form of the double-helical regions within the molecules by changing the buffer conditions. This result was supported by circular dichroic measurements. The A to A′ transition may have important consequences for RNA-protein interactions. [ABSTRACT FROM AUTHOR]

Published
1985
Full Text
View/download PDF

64. Conserved unpaired adenine residues are important for ordered structures of 5S ribosomal RNA. An infrared study of the secondary and tertiary structure of <em>Thermus thermophilus</em> 5S rRNA.

Author

Böhm, Siegfried, Venyaminov, Sergei Yu., Fabian, Heinz, Filimonov, Vladimir V., and Welfle, Heinz

Subjects
CALIBRATION, RNA, FUSION (Phase transformation), LOW temperatures, ADENINE
Abstract

An improved set of infrared calibration spectra for the determination of G · C and A · U base pairs leads to 32 ± 3 G · C (+G · U) and 4 ± 1 A · U base pairs for Thermus thermophilus 5S RNA in the presence and absence of Mg2+. These results give further support for the consensus secondary structure of 5S RNA recently proposed by several groups. T thermophilus 5S RNA shows, in the presence of Mg2+, a distinct two-step thermal melting of its ordered structure. Based on new data about the stacking dependence of infrared intensities of unpaired ribonucleotides the spectral changes of the low-temperature transition should be explained by melting of stacked arrangements of unpaired bases and/or non-standard base pairs. Striking is the reduction in A stacking, which is not related to the melting of A · U base pairs, indicating the importance of the mostly conserved unpaired adenines for the Mg2+ stabilized higher-order structures especially within internal loops of 5S RNA. [ABSTRACT FROM AUTHOR]

Published
1985

66. Interaction of fMet‐tRNAfMetwith the C‐terminal domain of translational initiation factor IF2 from Bacillus stearothermophilus

Author

Krafft, Christoph, Diehl, Annette, Laettig, Stefan, Behlke, Joachim, Heinemann, Udo, Pon, Cynthia L., Gualerzi, Claudio O., and Welfle, Heinz

Abstract

Analytical ultracentrifugation studies indicated that the C‐terminal domains of IF2 comprising amino acid residues 520–741 (IF2 C) and 632–741 (IF2 C‐2) bind fMet‐tRNA with similar affinities (Kdat 25°C equal to 0.27 and 0.23 μM, respectively). Complex formation between fMet‐tRNAfMetand IF2 C or IF2 C‐2 is accompanied by barely detectable spectral changes as demonstrated by a comparison of the Raman spectra of the complexes with the calculated sum of the spectra of the individual components. These results and the temperature dependence of the Kdof the protein–RNA complexes indicate that complex formation is not accompanied by obvious conformational changes of the components, and possibly depends on a rather small binding site comprising only a few interacting residues of both components.

Published
2000
Full Text
View/download PDF

67. Preliminary characterization by X‐ray diffraction and Raman spectroscopy of a crystalline complex of Bacillus stearothermophilusinitiation factor 2 C‐­domain and fMet‐tRNAfMet

Author

Förster, Charlotte, Krafft, Christoph, Welfle, Heinz, Gualerzi, Claudio O., and Heinemann, Udo

Abstract

Bacillus stearothermophilustranslation initiation factor 2 (IF2) specifically binds initiator fMet‐tRNAfMetand positions it into the ribosomal peptidyl site in the course of the initiation of protein biosynthesis. The isolated C‐terminal domain of IF2 is capable of binding fMet‐tRNAfMet, as shown by RNase A and hydrolysis protection experiments. In the presence of fMet‐tRNAfMet, the IF2 C‐domain yielded orthorhombic crystals of space group I222 (I212121) diffracting to 3.4 Å resolution. The existence of equimolar amounts of tRNA and protein in the crystals was proven by Raman spectroscopy. The observed unit cell suggests the presence of two IF2 C‐­domain–fMet‐tRNAfMetcomplexes per asymmetric unit of the crystal.

Published
1999
Full Text
View/download PDF

68. Contributory presentations/posters

Author

Manoj, N., Srinivas, V., Surolia, A., Vijayan, M., Suguna, K., Ravishankar, R., Suguna, K., Surolia, A., Vijayan, M., Schwarzenbacher, R., Zeth, K., Diederichs, Kostner, G., Gries, A., Laggner, P., Prassl, R., Madhusudan, Akamine, Pearl, Xuong, Nguyen-huu, Taylor, Susan, Sagar, M., Ravishankar, R., Saikrishnan, K., Roy, S., Purnapatre, K., Handa, P., Varshney, U., Vijayan, M., Biswal, B., Sukumar, N., Vijayan, M., Rao, J., Johnson, A., Pattabhi, Vasantha, Krishna, S., Sastri, Mira, Savithri, H., Murthy, M., Pillai, Bindu, Kannan, Hosur, M., Kumar, Mukesh, Patwardhan, Swati, Kannan, K., Hosur, M., Padmanabhaa, B., Sasaki-Sugio, S., Nukaga, M., Matsuzaki, T., Karthikevan, S., Sharma, S., Sharma, A., Paramasivam, M., Kumar, P., Khan, J., Yadav, S., Srinivasan, A., Singh, T., Gourinath, S., Alam, Neelima, Srintvasan, A., Singh, T., Chandra, Vikas, Kaur, Punit, Betzel, Ch., Singh, T., Ghosh, S., Bera, A., Bhattacharya, S., Chakraborty, S., Pal, A., Mukhopadhyay, B., Dey, I., Haldar, U., Baneriee, Asok, Sevcik, Jozef, Solovicova, Adriana, Sekar, K., Sundaralingam, M., Betzel, Ch., Genov, N., Singh, T., Liang, Dong-cai, Jiang, Tao, Zhang, Ji-ping, Chang, Wen-rui, Jahnke, Wolfgang, Blommers, Marcel, Panchal, S., Hosur, R., Pillay, Bindu, Hosur, M., Mathur, Puniti, Srivatsun, S., Joshi, Ratan, Jaganathan, N., Chauhan, V., Atreya, H., Sahu, S., Chary, K., Govil, Girjesh, Adjadj, Elisabeth, Quinjou, Éric, Izadi-Pruneyre, Nadia, Blouquit, Yves, Mispelter, Joël, Heyd, Bernadette, Lerat, Guilhem, Milnard, Philippe, Desmadreil, Michel, Lin, Y., Rao, B., Raghunathan, Vidva, Chau, Mei, Rao, B., Pesais, Prashant, Srivastava, Sudha, Coutinho, Evans, Saran, Anil, Sapico, Leizl, Gesme, Jayson, Lijima, Herbert, Paxton, Raymond, Srikrishnan, Thamarapu, Grace, C., Nagenagowda, G., Lynn, A., Cowsik, Sudha, Sahu, Sarata, Chauhan, S., Bhattacharya, A., Chary, K., Govil, G., Kumar, Anil, Pellecchia, Maurizio, Zuiderweg, Erik, Kawano, Keiichi, Aizawa, Tomoyasu, Fujitani, Naoki, Hayakawa, Yoichi, Ohnishi, Atsushi, Ohkubo, Tadayasu, Kumaki, Yasuhiro, Hikichi, Kunio, Nitta, Katsutoshi, Rani Parvathy, V., Chary, K., Kini, R., Govil, G., Koshiba, Takumi, Kobashigawa, Yoshihiro, Yao, Min, Demura, Makoto, Nakagawa, Astushi, Tanaka, Isao, Kuwajima, Kunihiro, Nitta, Katsutoshi, Linge, Jens, Donoghue, Seán, Nilges, Michael, Chakshusmathi, G., Ratnaparkhi, Girish, Madhu, P., Varadarajan, R., Tetreau, C., Tourbez, M., Lavalette, D., Manno, M., Biagio, P., Martorana, V., Emanuele, A., Vaiana, S., Bulone, D., Palma-Vittorelli, M., Palma, M., Trivedi, V., Cheng, S., Chien, W., Yang, S., Francis, S., Chang, D., Batra, Renn, Geeves, Michael, Manstein, Dietmar, Trvlska, Joanna, Grochowski, Pawel, Geller, Maciej, Ginalski, K., Grochowski, P., Lesyng, B., Lavalette, P., Tetreau, C., Tourbez, M., Blouquit, Y., Roccatano, D., Amadei, A., Nola, A., Berendsen, H., Ho, Bosco, Curmi, P., Berry, H., Lairez, D., Pauthe, E., Pelta, J., Kothekar, V., Sahi, Shakti, Srinivasan, M., Singh, Anil, Madhusudnan, Kartha, Nandel, Fateh, Kaur, Harpreet, Nandel, Fateh, Singh, Balwinder, Jain, D., Feenstra, K., Berendsen, Herman, Tama, F., Sanejouand, Y., Go, N., Sharma, Deepak, Sharma, Sunita, Pasha, Santosh, Brahmachari, Samir, Viiavaraghavan, R., Makker, Jyoti, Dey, Sharmisllia, Kumar, S., Singh, T., Lakshmikanth, G., Krishnamoorthy, G., Mazhul, V., Zaitseva, E., Kierdaszuk, Borys, Widengren, J., Terry, B., Mets, Ü., Rigler, R., Swaminathan, R., Thamotharan, S., Yathindra, N., Shibata, Y., Chosrowjan, H., Mataga, N., Morisima, I., Chakraharty, Tania, Xiao, Ming, Cooke, Roger, Selvin, Paul, Branca, C., Faraone, A., Magazù, S., Maisano, G., Migliardo, P., Villari, V., Behere, Digambar, Deva, M., Brunori, M., Cutruzzolà, F., Gibson, Q., Savino, C., Travaglini-Allocatelli, C., Vallone, B., Prasad, Swati, Mazumdar, Shyamalava, Mitra, Samaresh, Soto, P., Fayad, R., Sukovataya, I., Tyulkova, N., Mamedov, Sh., Aktas, B., Canturk, M., Aksakal, B., Yilgin, R., Bogutska, K., Miroshnichenko, N., Chacko, S., DiSanto, M., Hypolite, J., Zheng, Y-M., Wein, A., Wojciechowski, M., Grycuk, T., Antosiewicz, J., Lesyng, B., Ceruso, Marc, Nola, Alfredo, Bandvopadhvay, Subhasis, Chatterjee, Bishnu, Choudhury, Devapriva, Thompson, Andrew, Stojanoff, Vivian, Pinkner, Jerome, Hultgren, Scott, Khight, Stefan, Flatters, Delphine, Goodfellow, Julia, Takazawatt, Fumi, Kanehisa, Minoru, Sasai, Masaki, Nakamura, Hironori, Sasai, Masaki, Han, Wang, Zheng, Yuan, Xin, Wang, Min, Pan, Bhakuni, Vlnod, Kulkarni, Sangeeta, Ahmad, Atta, Prakash, Koodathingal, Prajapati, Shashi, Surin, Alexey, Matsumoto, Tomoharu, Yang, Li, Nakagawa, Yuki, Kimura, Kazumoto, Amemiya, Yoshiyuki, Semisotnov, Gennady, Kihara, Hiroshi, Tayyab, Saad, Muzammil, Salman, Kumar, Yogesh, Kulkarni, Sangeeta, Prajapati, Shashi, Prakash, Koodathingal, Ahmad, Atta, Bhakuni, Vinod, Sundd, Monica, Kundu, Suman, Jagannadham, M., Kundu, Suman, Sundd, Monica, Jagannadham, Medicherla, Chandani, Bina, Dhar, Ruby, Sinha, Lalankumar, Warrier, Deepti, Mehrotra, Sonam, Khandelwal, Purnima, Seth, Subhendu, Hosur, R., Sasidhar, Y., Prabha, C., Gidwani, Arun, Ahmad, Atta, Kulkarni, Sangeeta, Madhusudan, K., Bhakuni, Vinod, Kinjo, Akira, Nishikawa, Ken, Chakravarty, Suvobrata, Varadarajan, Raghavan, Noyelle, K., Haezebrouck, P., Joniau, M., Dael, H., Dash, Sheffali, Jha, Indra, Bhat, Rajiv, Mohanty, Prasanna, Bandyopadhyay, A., Sonawat, H., Rao, Ch., Datta, Siddhartha, Rajaraman, K., Raman, B., Ramakrishna, T., Rao, Ch., Pande, A., Pande, J., Betts, S., Asherie, N., Ogun, O., King, J., Benedek, G., Sokolova, I., Tyulkova, N., Kalacheva, G., Sonoyama, Masashi, Yokoyama, Yasunori, Taira, Kunihiro, Mitaku, Shigeki, Nakazawal, Chicko, Sasakil, Takanori, Mukai, Yuri, Kamo, Naoki, Sonoyama, Masashi, Mitaku, Shigeki, Dalal, Seema, Regan, Lynne, Mukai, Yuri, Kamo, Naoki, Mituku, Shigeki, Roychoudhury, Mihir, Kumar, Devesh, Lőrinczv, Dénes, Könczöl, Franciska, Farkas, László, Belagyi, Joseph, Schick, Christoph, Thomson, Christy, Ananthanarayanan, Vettai, Alirzayeva, E., Baba-Zade, S., Gromiha, M., Oobatake, M., Kono, H., An, J., Uedaira, H., Sarai, A., Takano, Kazufumi, Yamagata, Yuriko, Yutani, Katsuhide, Jas, Gouri, Muñoz, Victor, Hofrichter, James, Eaton, William, Penoyar, Jonathan, Srikrishnan, Thamarapu, Lo Verde, Philip, Kardos, J., Bódi, Á., Venekei, I., Závodszky, P., Gráf, L., Szilágyi, András, Závodszky, Péter, Allan, R., Walshaw, J., Woolfson, D., Funahashi, Jun, Takano, Kazufumi, Yamagata, Yuriko, Yutani, Katsuhide, Gupta, Savan, Mazumdar, Shyamalava, Di Nola, A., Mangoni, M., Roccatano, P., Ramachandraiah, Gosu, Chandra, Nagasuma, Kothekar, V., Srinivasan, M., Sahi, Shakti, Chakraborty, S., Bhattacharya, S., Bera, A., Ghosh, S., Pal, A., Haldar, U., Mukhopadhyay, B., Baneriee, Asok, Ciani, Barbara, Woolfson, Derek, Nair, Usha, Kaur, Kanwal, Salunke, Dinakar, Swaminathan, Chittoor, Surolia, Avadhesha, Rigler, R., Pramanik, A., Jonasson, P., Kratz, G., Jansson, O., Nygren, P., Ståhl, S., Ekberg, K., Johansson, B., Uhlén, S., Uhlén, M., Jörnvall, H., Wahren, J., Welfle, Karin, Misselwitz, Rolf, Höhne, Wolfgang, Welfle, Heinz, Mazhul, V., Zaitseva, E., Mitskevich, L., Fedurkina, N., Kurganov, B., Jarori, Gotam, Maity, Haripada, Guharay, J., Sengupta, B., Sengupta, P., Sridevi, K., Kasturi, S., Gupta, S., Agarwal, Gunjan, Kwong, Suzanne, Briehl, Robin, Ismailova, O., N, Tyulkova, Hariharan, C., Pines, D., Pines, E., Zamai, M., Cohen-Luria, R., Yayon, A., Parola, A., Padya, M., Spooner, G., Woolfeon, D., Bakshi, Panchan, Sharma, Deepak, Sharma, Sunita, Bharadwaj, D., Pasha, Santosh, Sharma, U., Srivastava, N., Barthwal, R., Jagannathan, N., Matsuda, Keiko, Nishioka, Takaaki, Go, Nobuhiro, Aita, T., Urata, S., Husimi, Y., Majumder, Mainak, Chatterjee, Bishnu, Abrescia, Nicola, Malinina, Lucy, Subirana, Juan, Aymami, Juan, Eritxa, Ramón, Coll, Miquel, Premraj, B., Yathindra, N., Thenmalarchelvi, R., Yathindra, N., Kumar, P., Gautham, N., Kan, Lou, Ming-Hou, Lin, Shwu-Bin, Sana, Tapas, Roy, Kanal, Bruant, N., Flatters, D., Lavery, R., Genest, D., Rons, Remo, Sklenar, Heinz, Lavery, Richard, Kundu, Sudip, Bhattacharyya, Dhananjay, Bandyopadhyay, Debashree, Thakur, Ashoke, Majumdar, Rabi, Barceló, F., Portugal, J., Ramanathan, Sunita, Chary, K., Rao, B., Gliosli, Mahua, Kumar, N., Varshney, Umesh, Chary, K., Pataskar, Shashank, Brahmachari, Samir, Sarojini, R., Selvasekarapandian, S., Kolandaivel, P., Sukumar, S., Selvasekarapandian, S., Sarojini, R., Kolmdaivel, P., Sukumar, S., Sarojini, R., Selvasekarapandian, S., Kolandaivel, P., Sukumar, S., Selvasekarapandian, S., Sarojini, R., Kolandaivel, P., Sukumar, S., Maiti, Motilal, Sen, Anjana, Das, Suman, Terra, Elisa, Suraci, Chiara, Diviacco, Silvia, Quadrifoglio, Franco, Xodo, Luigi, Bandyopadhyay, Debashree, Bhattacharyya, Dhananjay, Kundu, Sudip, Thakur, Ashoke, Das, Suman, Ray, Arghya, Maiti, Motilal, Karthikeyan, G., Chary, Kandala, Rao, Basuthkar, Mujeeb, Anwer, James, Thomas, Kasyanenko, N., Haya, E., Bogdanov, A., Zanina, A., Bugs, M., Cornélio, M., Srikrishnan, Thamarapu, Tolstorukov, M., Sanval, Nitish, Tiwari, S., Tiwari, S., Sanyal, Nitish, Choudhury, Mihir, Kumar, Devesh, Sanyal, Nitish, Patel, P., Bhavesh, Neel, Hosur, R., Gabrielian, Anna, Wennmalm, Stefan, Edman, Lars, Rigler, Rudolf, Constantinescu, B., Radu, L., Radulcscu, I., Gazdaru, D., Wärmländer, Sebastian, Leijon, Mikael, Aoki, Setsuyuki, Kondo, Takao, Ishiura, Masahiro, Pashinskaya, V., Kosevich, M., Shelkovsky, V., Blagoy, Yu., Wang, Ji-hua, Malathi, R., Chandrasekhar, K., Premraj, B., Patel, P., Kandimalla, E., Agrawal, S., Hosur, R., Yathindra, N., Rastogi, V., Palafox, M., Singh, Chatar, Beniaminov, A., Bondarenko, S., Zdobnov, E., Minyat, E., Ulyanov, N., Ivanov, V., Singh, J., Sonawane, Kailas, Grosjean, Henri, Tewari, Ravindra, Sonavane, Uddhavesh, Morin, Annie, Grosjean, Henri, Tewari, Ravindra, Doherty, Elizabeth, Doudna, Jennifer, Tochio, H., Sato, S., Matsuo, H., Shirakawa, M., Kyogoku, Y., Javaram, B., Dixit, Surjit, Shukla, Piyush, Kalra, Parul, Das, Achintya, McConnell, Kevin, Beveridge, David, Sawyer, W., Chan, R., Eccelston, J., Yan, Yuling, Davidson, B., Ray, Arghya, Tuite, Eimer, Norden, Bengt, Nielsen, Peter, Takahashi, Masayuki, Ghosh, Anirban, Bansal, Manju, Christ, Frauke, Thole, Hubert, Wende, Wolfgang, Pingoud, Alfred, Pingoud, Vera, Luthra, Pratibha, Chandra, Ramesh, Sen, Ranjan, King, Rodney, Weisberg, Robert, Larsen, Olaf, Berends, Jos, Heus, Hans, Hilbers, Cornelis, Stokkum, Ivo, Gobets, Bas, Grondelle, Rienk, Amerongen, Herbert, Sngrvan, HE., Babayan, Yu., Khudaverdian, N., Kono, H., Gromiha, M., Pichierri, F., Aida, M., Prabakaran, P., Sayano, K., An, J., Uedaira, H., Sarai, A., Serva, Saulius, Merkienė, Eglė, Vilkaitis, Giedrius, Weinhold, Elmar, Klimašauskas, Saulius, Marsich, Eleonora, Bandiera, Antonella, Xodo, Luigi, Manzini, Giorgio, Potikyan, G., Arakelyan, V., Babayan, Yu., Ninaber, Alex, Goodfellow, Julia, Ito, Yoichiro, Ohta, Shigeru, Husimi, Yuzuru, Usukura, J., Tagami, H., Aiba, H., Suarez, Mougli, Nunes, Elia, Keszenman, Deborah, Candreva, E., Nunes, Elia, Thyberg, Per, Földes-Papp, Zeno, Rigler, Rudolf, Joshi, Amita, Rao, Basuthkar, Singh, Dinesh, Rajeswari, M., Ira, Krishnamoorthy, G., Pregetter, M., Prassl, R., Schwarzenbacher, R., Amenitsch, H., Chapman, J., Laggner, P., Pandev, B., Mishra, K., Pohl, E., Sun, J., Agapov, I., Tonevitsky, A., Pohl, P., Dennison, S., Guharay, J., Sengupta, P., Gorbeako, G., Dynbko, T., Pappavee, N., Mishra, A., Manuel, Prieto, Rodrigo, Almeida, Luis, Loura, Gendel, L., Przestalski, S., Kuczera, J., Kleszczyńska, H., Kral, T., Chernitsky, E., Senkovich, O., Rosin, V., Allakhverdieva, Y., Papageorgiou, G., Gasanov, R., Apetrei, Calin, Savopol, Tudor, Balea, Marius, Cucu, D., Mihailescu, D., Ramanathan, K., Bačić, Goran, Sajot, Nicolas, Garnier, Norbert, Crouzy, Serge, Genest, Monique, Várkonyi, Z., Zsiros, O., Farkas, T., Combos, Z., Cribier, Sophie, Fraceto, I., Schreier, S., Spisni, A., Paula, F., Sevšek, F., Gomišček, G., Arrigler, V., Svetina, S., Žekš, B., Nomura, Fumimasa, Nagata, Miki, Takiguchi, Kingo, Hotani, Hirokazu, Panicker, Lata, Parvathanathan, P., Ishino, A., Saitoh, A., Hotani, H., Takiguchi, K., Afonin, S., Takahashi, A., Nakato, Y., Takizawa, T., Marathe, Dipti, Mishra, K., Jørgensen, Kent, Rawat, Satinder, Nair, Usha, Rukmini, R., Chattopadhyay, Amitabha, Šentiurc, M., Štrancar, J., Stolič, Z., Filipin, K., Pečar, S., Chattopadhyay, Amitabha, Biswas, S., Rukmini, R., Sana, Satyen, Samanta, Anunay, Kinoshita, Koji, Yamazaki, Masahito, Ohba, Tetsuhiko, Kiuchi, Tai, Yoshitoshi, Kamakura, Goto, Akira, Kumeta, Takaaki, Ohki, Kazuo, Sugar, I., Thompson, T., Thompson, K., Biltonen, R., Suezaki, Y., Ichinose, H., Takiguchi, K., Hotani, H., Akivama, M., Matuoka, S., Tsuchihashi, K., Gasa, S., Mattjus, P., Molotkovsky, J., Pike, H., Brown, R., Arora, Ashish, Kleinschmidt, Jörg, Tamm, Lukas, Luneva, O., Gendel, L., Kruglyakova, K., Fedin, V., Kuptsoya, O., Borst, J., Visser, N., Visser, A., Dyubko, T., Ogihara, Toshihiko, Mishima, Kiyoshi, Shvaleva, A., Radenović, N., Minić, P., Jeremić, M., Radenović, Č., Aripov, T., Tadjibaeva, E., Vagina, O., Zamaraeva, M., Salakhutdinov, B., Cole, A., Poppofl, M., Naylor, C., Titball, R., Basak, A., Eaton, J., Naylor, C., Justin, N., Moss, D., Titball, R., Basak, A., Nomura, F., Nagata, M., Ishjkawa, S., Takiguchi, K., Takahashi, S., Hotani, H., Obuchi, Kaoru, Staudegger, Erich, Kriechbaum, Manfred, Lehrer, Robert, Waring, Alan, Lohner, Karl, Gangl, Susanne, Mayer, Bernd, Köhler, Gottfried, Shobini, J., Mishra, A., Guttenberg, Z., Lortz, B., Hu, B., Sackmann, E., Kozlova, N., Lukyanenko, L., Antonovich, A., Slobozhanina, E., Chernitsky, E., Krylov, Andrey, Antonenko, Yuri, Kotova, Elena, Yaroslavov, Alexander, Ghosh, Subhendu, Bera, Amal, Das, Sudipto, Urbánková, Eva, Jelokhani-Niaraki, Masood, Freeman, Karl, Jezek, Petr, Usmanov, P., Ongarbaev, A., Tonkikh, A., Pohl, Peter, Saparov, Sapar, Harikumar, P., Reeves, J., Rao, S., Sikdar, S., Ghatpande, A., Rao, S., Sikdar, S., Corsso, C., Campos de Carvalho, A., Varanda, W., ElHamel, C., Dé, E., Saint, N., Molle, G., Varshney, Anurae, Mathew, M., Loots, E., Isacoff, E., Kasai, Michiki, Yamaguchi, Naohiro, Ghosh, Paramita, Ghosh, Subhendu, Tigyi, Joseph, Tigyi, Gabor, Liliom, Karoly, Miledi, Ricardo, Djurisic, Maja, Andjus, Pavle, Shrivastava, Indira, Sansom, M., Barrias, C., Oliveira, P., Mauricio, A., Rebelo da Costa, A., Lopes, I., Barrias, C., Fedorovich, S., Chubanov, V., Sholukh, M., Konev, S., Fedirko, N., Manko, V., Klevets, M., Shvinka, N., Prabhananda, B., Kombrabail, Mamata, Aravamudhan, S., Venegas-Cotero, Berenice, Blake, Ivan, Zhang, Zhi-hong, Hu, Xiao-jian, Zhou, Han-qing, Cheng, Wei-ying, Feng, Hang-fang, Dubitsky, L., Vovkanvch, L., Zalyvsky, I., Savio-Galimberti, E., Bonazzola, P., Ponce-Homos, J., Parisi, Mario, Capurro, Claudia, Toriano, Roxana, Ready, Laxma, Jones, Larry, Thomas, David, Tashmukhamedov, B., Sagdullaev, B., Usmanov, P., Mauricio, A., Heitzmann, D., Warth, R., Bleich, M., Greger, R., Ferreira, K., Ferreira, H., Zagoory, Orna, Alfahel, Essa, Parola, Abraham, Priel, Zvi, Hama-Inaba, H., Wang, R., Choi, K., Nakajima, T., Haginoya, K., Mori, M., Ohyama, H., Yukawa, O., Hayata, I., Joshi, Nanda, Kannurpatti, Sridhar, Joshi, Preeti, Sinha, Mau, Shen, Xun, Hu, Tianhui, Bei, Ling, Knetsch, Menno, Schäfers, Nicole, Manstein, Dietmar, Sandblom, John, Galvanovskis, Juris, Pologea-Moraru, Roxana, Kovacs, Eugenia, Savopol, Tudor, Dinu, Alexandra, Sanghvi, S., Mishra, K., Jazbinšek, V., Thiel, G., Müller, W., Wübeller, G., Tronteli, Z., Fajmut, Leš, Marhl, Marko, Brumen, Milan, Volotovski, I., Sokolovski, S., Knight, M., Vasil’ev, Alexei, Chalyi, Alexander, Sharma, P., Steinbach, P., Sharma, M., Amin, N., Barchir, J., Albers, R., Pant, H., Balasubramanyam, M., Condrescu, M., Reeves, J., Gardner, J., Monajembashi, Shamci, Pilarczyk, Gotz, Greulich, K., Kovacs, Eugenia, El-Refaei, F., Talaat, M., El-Awadi, A., Ali, F., Tahradník, Ivan, Pavelková, Jana, Zahradniková, Alexandra, Zhorov, Boris, Ananthanaravanan, Vettai, Michailov, M., Neu, E., Seidenbusch, W., Gornik, E., Martin, D., Welscher, U., Weiss, D., Pattnaik, B., Jellali, A., Forster, V., Hicks, D., Sahel, J., Dreyfus, H., Picaud, S., Wang, Hong-Wei, Sui, Sen-fang, Luther, Pradeep, Barry, John, Morris, Ed, Squire, John, Sundari, C., Balasubramanian, D., Veluraia, K., Christlet, T., Suresh, M., Berry, H., Pelta, J., Lairez, D., Laretta-Garde, V., Krilov, Dubravka, Stojanović, Nataša, Herak, Janko, Jasuja, Ravi, Ivanova, Maria, Mirchev, Rossen, Ferrone, Frank, Stopar, David, Spruijt, Ruud, Wolfs, Cor, Hemminga, Marcus, Arcovito, G., Spirito, M., Sui, Sen-fang, Wang, Hong-Wei, Agrawal, Rajendra, Heagle, Amy, Penczek, Pawel, Grassucci, Robert, Frank, Joachim, Sharma, Manjuli, Jeyakumar, Loice, Fleischer, Sidney, Wagenknecht, Terence, Knupp, Carlo, Munro, Peter, Luther, Pradeep, Ezra, Eric, Squire, John, Ichihara, Koji, Kitazawa, Hidefumi, Iguchi, Yusuke, Hotani, Hirokazu, Itoh, Tomohiko, Pifat, Greta, Kveder, Marina, Pečar, Slavko, Schara, Milan, Nair, Deepak, Singh, Kavita, Rao, Kanury, Salunke, Dinakar, Kaur, Kanwaljeet, Jain, Deepti, Sundaravadivel, B., Goel, Manisha, Salunke, D., Kovalenko, E., Semenkova, G., Cherenkevich, S., Lakshmanan, T., Sriram, D., Srinivasan, S., Loganathan, D., Ramalingam, T., Lebrón, J., Bjorkman, P., Singh, A., Gayatri, T., Jain, Deepti, Kaur, Kanwaljeet, Sundaravadivel, B., Salunke, Dinakar, Caffarena, Ernesto, Grigera, J., Bisch, Paulo, Kiessling, V., Fromherz, P., Rao, K., Gaikwad, S., Khan, M., Suresh, C., Kaliannan, P., Gromiha, M., Elanthiraiyan, M., Chadha, K., Payne, J., Ambrus, J., Nair, M., Nair, Madhavan, Mahajan, S., Chadha, K., Hewitt, R., Schwartz, S., Bourguignon, J., Faure, M., Cohen-Addad, C., Neuburger, M., Ober, R., Sieker, L., Macherel, D., Douce, R., Gurumurthy, D., Velmurugan, S., Lobo, Z., Srivastava, Sudha, Phadke, Ratna, Govil, Girjesh, Desai, Prashant, Coutinho, Evans, Guseinova, I., Suleimanov, S., Zulfugarov, I., Novruzova, S., Aliev, J., Ismayilov, M., Savchenko, T., Alieva, D., Ilík, Petr, Kouřil, Roman, Bartošková, Hana, Nauš, Jan, Gaikwad, Jvoti, Thomas, Sarah, Vidyasagar, P., Garab, G., Simidjiev, I., Rajagopal, S., Várkonyi, Zs., Stoylova, S., Cseh, Z., Papp, E., Mustárdy, L., Holzenburg, A., Bruder, R., Genick, U., Woo, T., Millar, D., Gerwert, K., Getzoff, E., Jávorfí, Tamás, Garab, Győző, Naqvi, K., Kalimullah, Md., Gaikwad, Jyoti, Thomas, Sarah, Semwal, Manoj, Vidyasagar, P., Kouril, Roman, Ilik, Petr, Naus, Man, Pomozi, István, Horváth, Gábor, Wehner, Rüdiger, Bernard, Gary, Damjanović, Ana, Ritz, Thorsten, Schulten, Klaus, Jushuo, Wang, Jixiu, Shan, Yandao, Gong, Tingyun, Kuang, Nanming, Zhao, Freiberg, Arvi, Timpmann, Kõu, Ruus, Rein, Woodbury, Neal, Nemtseva, E., Kudryasheva, N., Sizykh, A., Shikhov, V., Nesterenko, T., Tikhomirov, A., Forti, Giorgio, Finazzi, Giovanni, Furia, Alberto, Barbagallo, Romina, Forti, Giorgio, Iskenderova, S., Agalarov, R., Gasanov, R., Osamu, Miyashita, Nobuhiro, G., Soni, R., Ramrakhiani, M., Yagi, Hiromasa, Tozawa, Kacko, Sekino, Nobuaki, Iwabuchi, Tomoyuki, Yoshida, Masasuke, Akutsu, Hideo, Avetisyan, A., Kaulen, A., Skulachev, V., Feniouk, B., Breyton, Cécile, Kühlbrandt, Werner, Assarsson, Maria, Gräslund, Astrid, Zsiros, O., Horváth, G., Mustárdy, L., Libisch, B., Gombos, Z., Budagovskaya, N., Kudryasheva, N., Harada, Erisa, Fukuoka, Yuki, Ohmura, Tomoaki, Fukunishi, Arima, Kawai, Gota, Watanabe, Kimitsuna, Akutsu, Hideo, Derganc, Jure, Božič, Bojan, Svetina, Saša, Žekš, Boštjan, Hoh, J., Li, Z., Rossmanith, G., Beer, E., Treijtel, B., Frederix, P., Blangè, T., Hénon, S., Galtet, F., Laurent, V., Planus, E., Isabey, D., Rath, L., Dash, P., Raval, M., Ramakrishnan, C., Balaram, R., Randic, Milan, Basak, Subhash, Vracko, Marjan, Nandy, Ashesh, Amic, Dragan, Beslo, Drago, Nikolic, Sonja, Trinajstic, Nenad, Walahaw, J., Woolfson, D., Lensink, Marc, Berendsen, Herman, Reddy, Boojala, Shindylov, Ilya, Bourne, Philip, Donnamaria, M., Xammar Oro, J., Grigera, J., Neagu, Monica, Neagu, Adrian, Praprotnik, Matej, Janežič, Dušanka, Mark, Pekka, Nilsson, Lennart, Martorana, V., Bulone, D., Fata, L., Manno, M., Biagio, P., Dardenne, Laurent, Werneck, Araken, Neto, Marçal, Bisch, Paulo, Kannan, N., Vishveshwara, S., Christlet, T., Veluraja, K., Grunwald, Gregory, Balaban, Alexandra, Basak, Kanika, Gute, Brian, Mills, Denise, Opitz, David, Balasubramanian, Krishnan, Mihalas, G., Lungeanu, Diana, Macovievici, G., Gruia, Raluca, Neagu, Monica, Cortez-Maghelly, C., Dalcin, B., Passos, E., Blesic, S., Ljubisavljevic, M., Milosevic, S., Stratimirovic, D., Bachhawat, Nandita, Mande, Shekhar, Ghosh, S., Nandy, A., Saito, Ayumu, Nishigaki, Koichi, Nishigaki, Koichi, Naimuddin, Mohammed, Mitaku, Shigeki, Hirokawa, Takatsugu, Ono, Mitsuo, Takaesu, Hirotomo, El Gohary, M., Ahmed, Abdalla, Eissa, A., Nakashima, Hiroshi, Nishikawa, Ken, Neagu, Monica, Neagu, Adrian, Raghava, G., Kurgalvuk, N., Goryn, O., Gerstman, Bernard, Gritsenko, E., Remmel, N., Maznyak, O., Kratasyuk, V., Esimbekova, E., Kratasyuk, V., Tchitchkan, D., Koulchitsky, S., Tikhonov, A., German, A., Pesotskaya, Y., Pashkevich, S., Pletnev, S., Kulchitsky, V., Duvvuri, Umamaheswar, Charagundla, Sridhar, Rizi, Rahim, Leigh, John, Reddy, Ravinder, Kumar, Mahesh, Coshic, O., Julka, P., Rath, O., Jagannathan, NR., Iliescu, Karina, Sajin, Maria, Moisoi, Nicolcta, Petcu, Ileana, Kuzmenko, A., Morozova, R., Nikolenko, I., Donchenko, G., Rahman, M., Ahmed, M., Naimuddin, Mohammed, Watanabe, Takehiro, Nishigaki, Koichi, Rubin, Y., Gilboa, H., Sharony, R., Ammar, R., Uretzky, G., Khubchandani, M., Mallick, H., Kumar, V., Jagannathan, N., Borthakur, Arijitt, Shapiro, Erik, Begum, M., Degaonkar, Mahaveer, Govindasamy, S., Dimitrov, Ivan, Kumosani, T., Bild, W., Stefanescu, I., Titescu, G., Iliescu, R., Lupusoru, C., Nastasa, V., Haulica, I., Khetawat, Gopal, Faraday, N., Nealen, M., Noga, S., Bray, P., Ananieva, T., Lycholat, E., Pashinskaya, V., Kosevich, MV., Stepanyan, S., Lycholat, E., Ananieva, T., Antonyuk, S., Khachatryan, R., Arakelian, H., Kumar, A., Ayrapetyan, S., Mkheyan, V., Agadjanyan, S., Khachatryan, A., Rajan, S., Kabaleeswaran, V., Malathi, R., Gopalakrishnan, Geetha, Govindachari, T., Ramrakhiani, Meera, Lowe, Phillip, Badley, Andrew, Cullen, David, Hermel, H., Schmahl, W., Möhwald, H., Singh, Anil, Majumdar, Nirmalya, Das, Joydip, Madhusudnan, Kartha, Dér, András, Kelemen, Loránd, Oroszi, László, Hámori, András, Ramsden, Jeremy, Ormos, Pál, Savitri, D., Mitra, Chanchal, Yanagida, Toshio, Esaki, Seiji, Kimura, Yuji, Nishida, Tomoyuki, Sowa, Yosiyuki, Radu, M., Koltover, V., Estrin, Ya., Kasumova, L., Bubnov, V., Laukhina, E., Dotta, Rajiv, Degaonkar, M., Raghunathan, P., Jayasundar, Rama, Jagannathan, N., Novák, Pavel, Marko, Milan, Zahradník, Ivan, Hirata, Hiroaki, Miyata, Hidetake, Ohki, Kazuo, Balaji, J., Sengupta, P., Maiti, S., Gonsalves, M., Barker, A., Macpherson, J., O’Hare, D., Winlove, C., Unwin, P., Sengupta, P., Phillip, R., Banerjee, S., Kumar, G., Maiti, S., Nagayaka, K., Danev, R., Sugitani, S., Murata, K., Gősch, Michael, Blom, H., Thyberg, P., Földes-Papp, Z., Björk, G., Holm, J., Heino, T., Rigler, Rudolf, Yokochi, Masashi, Inagaki, Fuyuhiko, Kusunoki, Masami, Matthews, E., Pines, J., Chukova, Yu., Koltover, Vitaly, Bansal, Geetanjali, Singh, Uma, Bansal, M., Nakata, Kotoko, Nakano, Tastuya, Kaminuma, Tsuguchika, Kang, B., Singh, U., Kirn, Bonn, Potocnik, Neja, Stare, Vito, Shukla, Latal, Natarajan, V., Devasagayam, T., Sastry, M., Kesavan, P., Sayfutdinov, R., Adamovich, V., Rogozin, D., Degermendzhy, A., Khetrapal, C., Ramanathan, K., Gowda, G., Ghimire, Kedar, Masaru, Ishida, Fujita, H., Ishiwata, S., Kishimoto, Y., Kawahara, S., Suzuki, M., Mori, H., Mishina, M., Kirino, Y., Ohshima, H., Dukhin, A., Shilov, V., Goetz, P., Sengupta, B., Guharay, J., Sengupta, P., and Mishra, R.

Published
1999
Full Text
View/download PDF

69. Laser Raman studies of rat liver ribosomal 5 S RNA

Author

Reich Peter, Heinz Bielka, Heinz Fabian, Welfle Heinz, and Böhm Siegfried

Subjects
Stereochemistry, Guanine, Base pair, Biophysics, Stacking, Spectrum Analysis, Raman, Biochemistry, Ribosome, symbols.namesake, chemistry.chemical_compound, Structural Biology, Genetics, Animals, Molecular Biology, Chemistry, RNA, Hydrogen Bonding, Cell Biology, Ribosomal RNA, Protein tertiary structure, Rats, Molecular Weight, Liver, RNA, Ribosomal, symbols, Nucleic Acid Conformation, Raman spectroscopy
Abstract

The secondary and tertiary structure of ribosomal 5 S RNAs has been studied using a variety of physical and chemical techniques (review [ 11). As part of our spectroscopic investigations on ribosomal RNAs we report here on Raman spectroscopic data of the native form of 5 S RNA of rat liver ribosomes. Laser Raman spectroscopy has proved to be a sensitive probe for the structure of RNAs, especially for the determination of the type and extent of base stacking, the amount of order in the ribophosphate backbone and the percentage of U residues in base-paired regions [2-51. Raman data have been published for E. coli 5 S RNA [5] and yeast 5 S RNA [6]. Our Raman data for rat liver 5 S RNA indicate a very high regularity of the ribophosphate backbone in the native form of rat liver 5 S RNA, comparable to native tRNAs. The stacking efficiency of the guanine ba.ses is much higher in 5 S RNA than in yeast tRNAPhe, while that of the adenine bases is lower. The results support a base pairing pattern [7] which is very similar to that proposed in [8].

Published
1981

70. Laser Raman studies of the 5 S rRNA-protein L5 complex of rat liver ribosomes

Author

Fabian, Heinz, Böhm, Siegfried, Carius, Wolfgang, Misselwitz, Rolf, and Welfle, Heinz

Abstract

The effects of ribosomal protein L5 on the conformation of 5 S rRNA in the 5 S rRNA—protein L5 complex extracted from rat liver ribosomes have been studied by laser Raman spectroscopy. A comparison of the spectra shows small protein-induced conformational changes in the 5 S rRNA, but most of the base-paired regions appear to be present in the complex with protein L5 as well as in the free 5 S rRNA. Furthermore specific interactions between 5 S rRNA and protein L5 are indicated. Cytosine (and/or uracil) residues in single-stranded regions and the N(7) of guanine are engaged in interactions with the protein as suggested by the Raman data.

Published
1983
Full Text
View/download PDF

72. Conformational stability of the DNA-binding histone-like protein, HBsu, from Bacillus subtilis, and of the four HBsu variants [F29W], [F47W], [F50W] and [F79W]

Author

Welfle, Heinz, Welfle, Karin, Misselwitz, Rolf, Groch, Nicolas, and Heinemann, Udo

Abstract

AbstractFrom denaturation studies with urea a free energy ΔGuH2Oof unfolding of 49.8 kJ · mol−1at 25C was calculated for the histone-like DNA-binding protein HBsu from Bacillus subtilis.Unfolding was monitored by circular dichroism measurements observing the changes of the molar mean residue ellipticity [©] at 222 nm. For the calculation of ΔGua two-state model of unfolding, i.e. the unfolding of native dimers into unfolded monomers, was applied. The validity of this model in high ionic strength buffer was proven by measurements at different protein concentrations yielding the same ΔGuvalues. Four HBsu variants, each carrying one single point mutation ([F29W], [F47W], [F50W] and [F79W]) were analysed with respect to their stability against unfolding at increasing temperatures and urea concentrations. The ΔGuvalues of mutants were calculated using the two-state model and show a reduced stability of the variants [F29W], [F47W], [F50W] and [F79W] in comparison to the wild type HBsu with ΔΔGu values of -9.2 kJ·mol−1, -7.5 kJ·mol−1, -5.9 kJ· mol−1, and -7.5 kJ · mol−1, respectively. Similar Δ ΔGuvalues were obtained for the HBsu mutant proteins by thermal unfolding experiments.

Published
1993
Full Text
View/download PDF

73. Stability of Escherichia coliSingle-Stranded DNA Binding Protein (EcoSSB)

Author

Misselwitz, Rolf, Welfle, Karin, Curth, Ute, Urbanke, Claus, and Welfle, Heinz

Abstract

AbstractConformation and stability of EcoSSB, a single-stranded DNA binding protein encoded by Escherichia coli, were analyzed by circular dichroism and fluorescence measurements. From CD measurements at pH 7.5, EcoSSB can be classified as a protein with high α-helix and β-sheet content. The hydrophobicity of the environment of the tryptophan residues of the native protein is only marginally increased in comparison to the unfolded protein. The GdnHCl induced unfolding curves measured by CD and fluorescence are coincident and sigmoidal and show a monophasic transition. The stability of EcoSSB is concentration dependent and the unfolding behavior can be described as a two-state transition from the folded tetrameter to unfolded monomers. The mean values of free energy of dissociation and unfolding ΔGH2Ouare between 173 and 177 kJ · mo−1and the mean half concentration c1/2of GdnHCl of the transition curves are about 1.5 M and 1.7 M for protein concentrations of 0.1 mg. ml−1and 0.5 mg · ml−1, respectively.

Published
1995
Full Text
View/download PDF

81. The Influence of Mn2+ on DNA structure in the presence of Na+ ions: A Raman spectroscopic study

Author

M. Muntean, Cristina, Misselwitz, Rolf, and Welfle, Heinz

Abstract

The influence of Mn2+ ions on the structure of natural calf thymus DNA was studied by Raman spectroscopy. Measurements were done at room temperature and pH 6.2±0.2, in the presence of the physiological concentration of 150 mM Na+ ions, and in the presence of Mn2+ concentrations that varied between 0 and 600 mM. No condensation of DNA was observed at any of the Mn2+ concentrations. At 5 mM Mn2+ and 150 mM Na+ no significant influence of Mn2+ ions on the DNA structure can be observed. Compared with our previous results obtained at 10 mM Na+ ions, binding of Mn2+ ions to charged phosphate groups and to DNA bases is inhibited in the presence of 150 mM Na+ ions. DNA backbone conformational changes were not observed in the whole concentration range of Mn2+ ions as judging from the Raman spectra. No evidence for DNA melting was identified. A high Mn2+ affinity for binding to guanine N7 and possibly, in a much lesser extent, to adenine have been found.

Published
2006
Full Text
View/download PDF

82. Mn2+–DNA interactions in aqueous systems: A Raman spectroscopic study

Author

M. Muntean, Cristina, Misselwitz, Rolf, Dostál, Lubomir, and Welfle, Heinz

Abstract

Interaction of natural calf thymus DNA with Mn2+ ions was studied by means of Raman spectroscopy. Spectra of DNA in 10 mM Na-cacodylate buffer, pH 6.2, 10 mM NaCl and in buffer containing Mn2+ ions were measured at room temperature. Mn2+ concentrations varied between 0 and 0.6 M. DNA backbone conformational changes and DNA denaturation were not observed in the concentration range 0 and 0.5 M, however, DNA condensation was observed at a critical concentration of 100 mM Mn2+ that prevented the measurement of Raman spectra. Binding of Mn2+ to the charged phosphate groups of DNA is indicated in the spectra. A high affinity of Mn2+ for guanine N7 was obvious, and binding to adenine was barely suggested.

Published
2006
Full Text
View/download PDF

83. Raman spectroscopy of regulatory protein Omega from Streptococcus pyogenes plasmid pSM19035 and complexes with operator DNA

Author

Dostál, Lubom?r, Misselwitz, Rolf, Laettig, Stefan, C. Alonso, Juan, and Welfle, Heinz

Abstract

pSM19035-encoded homodimeric ? protein (?2) regulates transcription of genes required for control of plasmid copy number and stable inheritance. ?2 belongs to the MetJ/Arc structural superfamily of repressors forming a ribbon-helix-helix (RHH) DNA binding motif, and binds specifically to operator regions containing at least two consecutive copies of heptad sequences 5'-A/TATCACA/T-3' in direct or inverted orientation. Solution properties of a double stranded 19 base-pairs oligonucleotide designed to model an operator DNA binding site of ?2 (top strand 5'-GCG AATCACA TGTGATT GG-3'), ?2, and the ?2:19-bp DNA complex were analysed by Raman spectroscopy. The Raman data indicate a sequence specific induced fit of both interacting macromolecules with ?2 binding to the major groove of the DNA, large perturbations of the DNA attributable to base unstacking, changes in vibrational modes of deoxyribose moieties, and protein-induced DNA bending. Protein marker bands indicate that a-helices are preserved, whereas amino acid side chains are largely perturbed, and unordered structures and turns become extensively restructured. Raman difference bands are consistent with interactions of thymine, adenine and cytosine with ?2 side chains. The results suggest that the central TCA/TGA stretch of the heptads might be the main target site for ?2 binding to operator DNA.

Published
2003
Full Text
View/download PDF

84. The structure of the anti-c-myc antibody 9E10 Fab fragment/epitope peptide complex reveals a novel binding mode dominated by the heavy chain hypervariable loops.

Author

Krauss N, Wessner H, Welfle K, Welfle H, Scholz C, Seifert M, Zubow K, Aÿ J, Hahn M, Scheerer P, Skerra A, and Höhne W

Subjects
Amino Acid Sequence, Calorimetry, Cell Line, Complementarity Determining Regions chemistry, Crystallography, X-Ray, Humans, Hydrogen Bonding, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Thermodynamics, Antibodies chemistry, Epitopes chemistry, Immunoglobulin Variable Region chemistry, Peptides chemistry, Proto-Oncogene Proteins c-myc immunology
Abstract

The X-ray structure of the Fab fragment from the anti-c-myc antibody 9E10 was determined both as complex with its epitope peptide and for the free Fab. In the complex, two Fab molecules adopt an unusual head to head orientation with the epitope peptide arranged between them. In contrast, the free Fab forms a dimer with different orientation. In the Fab/peptide complex the peptide is bound to one of the two Fabs at the "back" of its extended CDR H3, in a cleft with CDR H1, thus forming a short, three-stranded antiparallel beta-sheet. The N- and C-terminal parts of the peptide are also in contact with the neighboring Fab fragment. Comparison between the CDR H3s of the two Fab molecules in complex with the peptide and those from the free Fab reveals high flexibility of this loop. This structural feature is in line with thermodynamic data from isothermic titration calorimetry.

Published
2008
Full Text
View/download PDF

85. Conformation and stability of the Streptococcus pyogenes pSM19035-encoded site-specific beta recombinase, and identification of a folding intermediate.

Author

Bhardwaj A, Welfle K, Misselwitz R, Ayora S, Alonso JC, and Welfle H

Subjects
Bacterial Proteins genetics, Bacterial Proteins metabolism, Calorimetry, Differential Scanning, Circular Dichroism, DNA Nucleotidyltransferases genetics, DNA Nucleotidyltransferases metabolism, Dimerization, Enzyme Stability, Protein Conformation, Protein Denaturation, Protein Folding, Spectrometry, Fluorescence, Streptococcus pyogenes genetics, Urea chemistry, Bacterial Proteins chemistry, DNA Nucleotidyltransferases chemistry, Plasmids genetics, Streptococcus pyogenes metabolism
Abstract

Solution properties of beta recombinase were studied by circular dichroism and fluorescence spectroscopy, size exclusion chromatography, analytical ultracentrifugation, denaturant-induced unfolding and thermal unfolding experiments. In high ionic strength buffer (1 M NaCl) beta recombinase forms mainly dimers, and strongly tends to aggregate at ionic strength lower than 0.3 M NaCl. Urea and guanidinium chloride denaturants unfold beta recombinase in a two-step process. The unfolding curves have bends at approximately 5 M and 2.2 M in urea and guanidinium chloride-containing buffers. Assuming a three-state unfolding model (N2-->2I-->2U), the total free energy change from 1 mol of native dimers to 2 mol of unfolded monomers amounts to deltaG(tot) = 17.9 kcal/mol, with deltaG(N2-->2I) = 4.2 kcal/mol for the first transition and deltaG(I-->U) = 6.9 kcal/mol for the second transition. Using sedimentation-equilibrium analytical ultracentrifugation, the presence of beta recombinase monomers was indicated at 5 M urea, and the urea dependence of the circular dichroism at 222 nm strongly suggests that folded monomers represent the unfolding intermediate.

Published
2006
Full Text
View/download PDF

86. Role of the N-terminal region and of beta-sheet residue Thr29 on the activity of the omega2 global regulator from the broad-host range Streptococcus pyogenes plasmid pSM19035.

Author

Welfle K, Pratto F, Misselwitz R, Behlke J, Alonso JC, and Welfle H

Subjects
Bacterial Proteins chemistry, Bacterial Proteins genetics, Calorimetry, Differential Scanning, Circular Dichroism, DNA Footprinting, DNA, Bacterial metabolism, DNA-Binding Proteins chemistry, DNA-Binding Proteins genetics, Models, Molecular, Operator Regions, Genetic, Protein Binding, Protein Denaturation, Protein Folding, Protein Structure, Secondary, Repressor Proteins chemistry, Repressor Proteins genetics, Streptococcus pyogenes metabolism, Structure-Activity Relationship, Thermodynamics, Threonine chemistry, Threonine metabolism, Urea chemistry, Bacterial Proteins metabolism, DNA-Binding Proteins metabolism, Plasmids genetics, Repressor Proteins metabolism, Streptococcus pyogenes genetics
Abstract

The dimeric regulatory protein wild-type omega (wt omega2) binds to arrays of 7-bp sequences (heptads) present in the operator DNA region of copy control and partition functions of plasmid pSM19035. Each omega2 protein probably binds with an antiparallel beta-sheet structure in the major groove of the 7-bp subsite of the operator DNA. Exchange of threonine at position 29 to alanine (T29A) drastically affects the activity of variant protein omega2T29A both in vivo and in vitro, and reduces the thermodynamic stability deltaG(o)u, but does not change the conformation. Likewise, the binding affinity to DNA is reduced and the association of the two monomeric subunits of the omega2T29A dimer is weakened, as manifested by an increase in the dissociation constant from 3.2 microM for wt omega2 to 6.3 microM for omega2T29A. Denatured dimers are formed upon thermal unfolding of wt omega2 and omega2T29A at ca. 45 microM (D(n)<-->D(u)). Removal of 8 (omega2deltaN8), or even 18 (omega2deltaN18) N-terminal amino acids has no obvious effect either on the core structure or on the activity in comparison to wt omega2. The stability of variants omega2deltaN8 and omega2deltaN18 is similar to that of wt omega2, and their binding to operator DNA is not impaired.

Published
2005
Full Text
View/download PDF

87. Recognition of DNA by omega protein from the broad-host range Streptococcus pyogenes plasmid pSM19035: analysis of binding to operator DNA with one to four heptad repeats.

Author

de la Hoz AB, Pratto F, Misselwitz R, Speck C, Weihofen W, Welfle K, Saenger W, Welfle H, and Alonso JC

Subjects
Bacterial Proteins chemistry, Bacterial Proteins genetics, Base Sequence, Binding Sites, Circular Dichroism, DNA Footprinting, DNA, Bacterial chemistry, Deoxyribonuclease I metabolism, Electron Spin Resonance Spectroscopy, Gene Expression Regulation, Bacterial, Hydroxyl Radical metabolism, Kinetics, Models, Molecular, Molecular Sequence Data, Nucleic Acid Conformation, Protein Binding, Protein Conformation, Repressor Proteins chemistry, Repressor Proteins metabolism, Response Elements genetics, Thermodynamics, Bacterial Proteins metabolism, DNA, Bacterial metabolism, Operator Regions, Genetic genetics, Plasmids genetics, Repetitive Sequences, Nucleic Acid genetics, Streptococcus pyogenes genetics
Abstract

pSM19035-encoded omega protein forms a dimer (omega2) that binds to a set of 7-bp repeats with sequence 5'-NATCACN-3'. Upon binding to its cognate sites, omega2 regulates transcription of genes required for copy number control and stable inheritance of plasmids, and promotes accurate plasmid segregation. Protein omega2 binds poorly to one heptad but the affinity to DNA increases with two and more unspaced heptads in direct or inverted orientation. DNA titration of increasing numbers of heptads with omega2, monitored by circular dichroism measurements, indicates the binding of one omega2 to one heptad (omega2:heptad stoichiometry of 1:1). Spacing of two directly or inversely oriented heptads by 1 to 7 bp reduces the affinity of the protein for its cognate target site. The binding affinity of omega2 for two directly repeated heptads was severely reduced if one of the base pairs of the core 5'-ATCAC-3' sequence of one of the heptads was individually substituted by any other base pair. Hydroxyl radical footprinting shows a protection pattern at the 5'-ATCAC-3' core. These data suggest that each heptad defines an operator half-site and that tight binding of the symmetric omega2 to the central 5'-TCA-3' core of symmetric or asymmetric targets (differently oriented heptads) is probably achieved by structural changes of DNA and/or protein or both.

Published
2004
Full Text
View/download PDF

88. In vitro and in vivo stability of the epsilon2zeta2 protein complex of the broad host-range Streptococcus pyogenes pSM19035 addiction system.

Author

Camacho AG, Misselwitz R, Behlke J, Ayora S, Welfle K, Meinhart A, Lara B, Saenger W, Welfle H, and Alonso JC

Subjects
Algorithms, Bacillus subtilis drug effects, Chemical Phenomena, Chemistry, Physical, Chromatography, Gel, Circular Dichroism, Crystallography, X-Ray, Escherichia coli drug effects, Half-Life, Hydrogen-Ion Concentration, Molecular Weight, Plasmids genetics, Protein Folding, Spectrometry, Fluorescence, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Streptococcus pyogenes chemistry, Ultracentrifugation, Urea chemistry, Streptococcus pyogenes genetics
Abstract

Streptococcus pyogenes pSM19035-encoded epsilon (10.7 kDa) and zeta (32.4 kDa) proteins are necessary to secure stable plasmid inheritance in bacteria, with zeta acting as toxin that kills plasmid-deprived cells and epsilon as an antitoxin that neutralises the activity of zeta. The epsilon and zeta proteins co-purify as a stable complex that, according to analytical ultracentrifugation and gel filtration, exists as epsilon2zeta2 heterotetramer in solution. Co-crystals of the epsilon2zeta2 complex contain epsilon and zeta in 1:1 molar ratio. Unfolding studies monitoring circular dichroic and fluorescence changes show that the zeta protein has a significantly lower thermodynamic stability than the epsilon protein both in free state and in the complex. Proteolytic studies indicate that zeta protein is more stable in the epsilon2zeta2 complex than in the free state. In vivo studies reveal a short half-life of the epsilon antitoxin (-18 min) and a long lifetime of the zeta toxin (>60 min). When transcription-translation of a plasmid containing the epsilon and zeta genes was inhibited, cell death was observed after a short lag phase that correlates with the disappearance of the epsilon protein from the background.

Published
2002
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results