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Your search keyword '"Masashi Sonoyama"' showing total 145 results
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145 results on '"Masashi Sonoyama"'

102. 1B1512 Decay kinetics of the M photointermediate of bacteriorhodopsin in short chain phosphatidylcholine micelles(Membrane Proteins 1,The 49th Annual Meeting of the Biophysical Society of Japan)

Author

Masashi Sonoyama, Takashi Kikukawa, Makoto Demura, Yumiko Kuwabara, and Mina Fukumoto

Subjects
chemistry.chemical_compound, Membrane protein, chemistry, Chain (algebraic topology), biology, Phosphatidylcholine, Kinetics, Biophysics, biology.protein, Bacteriorhodopsin, Micelle
Published
2011
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103. 1P118 Structural stability and photocycle of bacteriorhodopsin in short chain phospholipid micelles(Membrane proteins,The 48th Annual Meeting of the Biophysical Society of Japan)

Author

Takashi Kikukawa, Makoto Demura, Masashi Sonoyama, Mina Fukumoto, and Yumiko Kuwabara

Subjects
chemistry.chemical_compound, chemistry, Biochemistry, Membrane protein, biology, Chain (algebraic topology), Structural stability, Phospholipid, biology.protein, Biophysics, Bacteriorhodopsin, Micelle
Published
2010
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104. First Observation of Precursory Structural Changes of Aliphatic Parts in the α-γ Polymorphic Transition of DL-Norleucine by Temperature-Scanning Time-Resolved FT-IR Spectroscopy

Author

Masayuki Matsumoto, Itaru Tsukushi, Masashi Sonoyama, Tadahiro Ishii, Tatsuhiko Nakano, and Hirofumi Yajima

Subjects
chemistry.chemical_compound, Crystallography, Transition (genetics), Chemistry, Norleucine, Ft ir spectroscopy, Analytical chemistry, General Chemistry, Spectroscopy
Abstract

Polymorphic transition of DL-norleucine from the α-form to the γ-form was investigated with temperature-scanning time-resolved FT-IR spectroscopy. The dynamic FT-IR measurements revealed the precursory structural changes in the aliphatic parts prior to the main overall polymorphic transition.

Published
2000
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106. 1P-028 Bisphenol A weakens Calcium Binding Affinity of Calmodulin(Protein:Structure & Function, The 47th Annual Meeting of the Biophysical Society of Japan)

Author

Masayuki Nara, Yasunori Yokoyama, Masashi Sonoyama, Sadayuki Matsuda, Koichi Murayama, Tomoyoshi Terada, and Yasuo Asami

Subjects
Bisphenol A, chemistry.chemical_compound, chemistry, Biochemistry, Calmodulin, biology, biology.protein, chemistry.chemical_element, Protein structure function, Calcium
Published
2009
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110. 3P-086 Identification of cytoplasmic and extracellular side of bacteriorhodopsin for force spectroscopy(Membrane proteins,The 47th Annual Meeting of the Biophysical Society of Japan)

Author

Yosuke Higashi, Naoya Watanabe, Yasunori Yokoyama, Masashi Sonoyama, Satoshi Ozaki, and Shigeki Mitaku

Subjects
Membrane protein, Cytoplasm, Extracellular, biology.protein, Force spectroscopy, Biophysics, Bacteriorhodopsin, Identification (biology), Biology, Cell biology
Published
2009
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117. 3P026 Effect of the filament concentrations on Raman optical activity of L-type straight flagellar filaments of Salmonella(Proteins-structure and structure-function relationship,Poster Presentations)

Author

Yoshiaki Hamada, Kenji Oosawa, Fumio Hayashi, Tomonori Uchiyama, and Masashi Sonoyama

Subjects
Protein filament, Salmonella, Crystallography, Protein structure, Chemistry, Structure function, medicine, Raman optical activity, medicine.disease_cause
Published
2007
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122. 2P163 Effect of Ion Concentration on Regeneration of Bacteriorhodopsin from Bacterio-opsin and All-trans Retinal(34. Membrane protein,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

Author

Shigeki Mitaku, Masashi Sonoyama, Hiroyuki Sugiyama, and Naoki Koito

Subjects
chemistry.chemical_compound, Opsin, chemistry, biology, Biochemistry, Membrane protein, Regeneration (biology), Biophysics, biology.protein, All trans, Retinal, Bacteriorhodopsin, Session (computer science)
Published
2006
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124. 1P377 Discrimination of G-protein by analyzing physicochemical properties of N- and C- terminal regions of G-proteins(15. Cellular signal transduction,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

Author

Kenichiro Imai, Ganga D. Ghimire, Fumitsugu Akazawa, Toshiyuki Tsuji, Masashi Sonoyama, and Shigeki Mitaku

Subjects
Terminal (electronics), G protein, Chemistry, Session (computer science), Bioinformatics, Cellular signal transduction, Cell biology
Published
2006
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127. 2P311 Amino acid sequence analysis of beta-barrel transmembrane proteins

Author

Kenichiro Imai, Naoyuki Asakawa, Ayano Ino, Masashi Sonoyama, Toshiyuki Tsuji, and Shigeki Mitaku

Subjects
chemistry.chemical_classification, Transmembrane domain, Beta barrel, Amino acid sequence analysis, Biochemistry, chemistry, Protein targeting, medicine, medicine.disease_cause, Peptide sequence, Transmembrane protein, Amino acid
Published
2005
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136. Effect of Carbonic Anhydrase II in Molten Globule State on Physical Properties of Dimyristoylphosphatidylcholine Liposome

Author

Hiroko Sakai, Michiko Tanaka, Kenichiro Imai, Masashi Sonoyama, and Shigeki Mitaku

Subjects
Liposome, Lysis, Carbonic anhydrase II, Inorganic chemistry, technology, industry, and agriculture, General Engineering, Membrane structure, General Physics and Astronomy, Molten globule, chemistry.chemical_compound, Membrane, chemistry, Biophysics, Pyrene, lipids (amino acids, peptides, and proteins), Lipid bilayer
Abstract

Ultrasonic relaxation measurement was employed for confirmation of the interaction between dimyristoylphosphatidylcholine (DMPC) membrane and a soluble protein, carbonic anhydrase II (CA II). The enhancement of the fluctuation of DMPC membrane structure was observed in the presence of CA II under acidic condition, pH 3.6–4, indicating the interaction between DMPC and CA II. The pyrene fluorescence spectrum of CA II solution clearly showed that this protein adopted an unfolding intermediate called the molten globule state under the low pH condition, in which CA II interacted with DMPC. However, CA II in the molten globule state did not cause membrane lysis in contrast to the high lytic activity of α-lactalbumin on DMPC liposomes.

Published
2001
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137. Ultrasonic Properties of a Binary System of a Soluble Protein, α-Lactalbumin and Dimyristoyl Phosphatidylcholine Membrane

Author

Hiroko Sakai, Masashi Sonoyama, Shigeki Mitaku, Michiko Tanaka, and Kenichiro Imai

Subjects
Lactalbumin, Phase transition, Liposome, Chromatography, Transition temperature, technology, industry, and agriculture, General Engineering, General Physics and Astronomy, chemistry.chemical_compound, Membrane, chemistry, Phosphatidylcholine, lipids (amino acids, peptides, and proteins), Binary system, Lipid bilayer
Abstract

The interaction between a soluble protein α-lactalbumin (α-LA) and dimyristoyl phosphatidylcholine (DMPC) liposomes was studied using an ultrasonic technique. The ultrasonic properties of DMPC liposomes changed significantly after the addition of α-LA at pH 3. The lipid bilayer transition temperature became higher and transition anomalies of DMPC liposomes were enhanced in the presence of α-LA under these conditions. At the same time, the size of the liposomes apparently decreased as revealed by the clearing of suspensions.

Published
2000
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143. An Origin of Complicated Infrared Spectra of Perfluoroalkyl Compounds Involving a Normal Alkyl Group.

Author

Takeshi Hasegawa, Takafumi Shimoaka, Yuki Tanaka, Nobutaka Shioya, Kohei Morita, Masashi Sonoyama, Hideki Amii, Toshiyuki Takagi, and Toshiyuki Kanamori

Abstract

Perfluoroalkyl (Rf) compounds containing a normal alkyl group often yield highly complicated infrared (IR) spectra especially in the C-F stretching vibration (ʋC-F) region. To reveal the reason behind this, the IR p-polarized multiple-angle incidence resolution spectrometry (pMAIRS) is employed to measure a monolayer of CF3(CF2)9(CH2)3COOH deposited on a silicon substrate. The compound is known to spontaneously aggregate to form a molecular assembly with the closest packing, in which the molecules are oriented perpendicular to the substrate. The IR pMAIRS spectra apparently prove that the complexity of the ʋC-F region is due to the normal alkyl part directly connected to the Rf group because the carbons in the Rf group are vibrated as a coupled oscillator, and the oscillation of the alkyl part propagates to the Rf part along the molecular axis. [ABSTRACT FROM AUTHOR]

Published
2015
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144. Effect of Partial Fluorination in the Myristoyl Groups on Thermal and Interfacial Properties of Dimyristoylphosphatidylcholine.

Author

Masaru Yoshino, Hiroshi Takahashi, Toshiyuki Takagi, Teruhiko Baba, Kohei Morita, Hideki Amii, Toshiyuki Kanamori, and Masashi Sonoyama

Abstract

A novel partially fluorinated analog of DMPC, diF4H10-PC, was synthesized, and its thermal and interfacial properties were compared with those of DMPC. By fluorine substitution in the terminal butyl segment in the myristoyl group of DMPC, the novel partially fluorinated diF4H10-PC membrane shows higher stability and larger occupied area, while remarkable decrease in the phase transition temperature and more hydrophilic properties in the hydrophilic/hydrophobic interface region were observed. [ABSTRACT FROM AUTHOR]

Published
2012
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145. SOSUI-GramN: high performance prediction for sub-cellular localization of proteins in Gram-negative bacteria

Author

Toshiyuki Tsuji, Kenichiro Imai, Shigeki Mitaku, Masashi Sonoyama, Ayano Ino, Naoyuki Asakawa, and Fumitsugu Akazawa

Subjects
amino acids, Gram-negative bacteria, biology, physicochemical parameters, General Medicine, Periplasmic space, Hypothesis, biology.organism_classification, Subcellular localization, Bioinformatics, Biochemistry, SOSUI, parasitic diseases, Extracellular, Inner membrane, Bacterial outer membrane, subcellular localization of proteins, Cellular localization
Abstract

A predictive software system, SOSUI-GramN, was developed for assessing the subcellular localization of proteins in Gram-negative bacteria. The system does not require the sequence homology data of any known sequences; instead, it uses only physicochemical parameters of the N- and C-terminal signal sequences, and the total sequence. The precision of the prediction system for subcellular localization to extracellular, outer membrane, periplasm, inner membrane and cytoplasmic medium was 92.3%, 89.4%, 86.4%, 97.5% and 93.5%, respectively, with corresponding recall rates of 70.3%, 87.5%, 76.0%, 97.5% and 88.4%, respectively. The overall performance for precision and recall obtained using this method was 92.9% and 86.7%, respectively. The comparison of performance of SOSUI-GramN with that of other methods showed the performance of prediction for extracellular proteins, as well as inner and outer membrane proteins, was either superior or equivalent to that obtained with other systems. SOSUI-GramN particularly improved the accuracy for predictions of extracellular proteins which is an area of weakness common to the other methods.

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