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The article offers information on the development of method for rapid reversed-phase high performance liquid chromatography (HPLC) for analysis of granulocyte colony stimulating factor (GCSF) for process analytical technology (PAT) applications. It also highlights an approach for development of on-line HPLC method and refolding dilution experiment. It mentions the role of several reagents in the study of HPLC including Trifiuoroacetic acid, acetonitrile and methanol.

The article highlights the 21st Symposium of the Protein Society held in Boston, Massachusetts. In keeping with the theme "Proteins: From Birth to Death," scientists discussed the biosynthesis, folding, signaling and degradation of proteins. Many presenters traced parts of the life story of proteins. The symposium was chaired by biologist Judith Frydman.

The article describes the development of the amide hydrogen-deuterium exchange method for screening protein stabilities in chromatography. The method is a protein-labeling technique sensitive to changes in tertiary structure that has been employed extensively to study conformational changes in a variety of protein-folding studies in solution. It may be used with chromatographic materials to identify buffer and resin conditions that are destabilizing to specific proteins.

Reports on the improvement of computational methods that can predict the structure of a protein from its amino acid sequence. Dependence of the biological function of a protein on the protein folding into the correct structure; Use of a computer program called Rosetta for modeling macromolecular structures and interactions. INSETS: Structural Alignment;Protein Structure Space.

Focuses on the development of arrays of diverse proteins printed on glass slides or silicon chips. Importance of the proper folding in chemically diverse structures of protein arrays; Production of antibodies for attachment to arrays; Identification of antigenic proteins in the genome of the pathogen. INSET: Glimpsing the Future . . . . . . . . . . ..

Reports the American Chemical Society convention in Chicago, Illinois. Strategies in protein folding and nuclear magnetic resonance (NMR) calculations; Computation of NMR spectra of atoms in various environment; Effects of solvent on the molecule's structure and behavior.

Reports on the International Conference on Protein Folding & Design held at the National Institutes of Health campus in Bethesda, Maryland in April 1996. Chemist Christian B. Anfinsen as honoree of the conference; Protein chemistry and biology topics covered by the conference; Intense inquiry into exactly how proteins change from unfolded forms into biologically active three-dimensional structures.

Features the efforts of researches to solve the protein-folding problem by developing computer programs to predict structures of folded proteins. Features of LINUS, a program developed by professor George D. Rose and postdoctoral fellow Rajgopal Srinivasan; Complementary program developed by professor Kenneth A. Dill and coworkers. INSET: Protein structure predictions available on World Wide Web..

The article focuses on the potential of drugs containing anti-amyloid accumulation properties to cure degenerative diseases. Researchers are aiming to develop drugs that act against accumulation of misfolded and aggregated proteins in areas of the brain. Jefferey W. Kelly of Scripps Research Institute discusses the actions of anti-amyloids such as their capability to stabilize the native state of an aggregation-prone protein, reduce the concentration of amyloid-forming, and remove toxic oligomers.

An interview with Kayatangi Prize winner Erik Demaine is presented. He notes that computational complexity theory is inapplicable for games like Chess, Checkers and Go, however there is an algorithmic solution to Nim. Demaine is engaged in solving protein folding. He also shares his works on geometry, algorithms and foldings and their impact on the modern life.

An interview with Christos Papadimitriou, 2008's recipient of the Katyanagi Prize for Research Excellence, is presented. When asked about his award, he thought he was just invited to speak at the ceremony and was not aware of his nomination. He views his work on protein folding as a very hard problem to solve, except that evolution has chose the proteins that know how to solve it. An overview of his notes concerning the future of programmers is also offered.

The article reports on the findings of the new stratum of meaning in the genetic code by scientists. Synonymous codons are discovered to influence the temporal pattern by which a messenger RNA molecule bearing genetic specifications from a nucleus of a cell is translated by machinelike ribosomes into protein molecules. The RNA-to-protein translation process generates unexpected changes, like the change of timing in nascent proteins folding when they elongates and peel away from ribosomes.

The article describes the compaction of DNA in the human cell by a factor of 10,000 into a nucleus, Chromosomes and protein complexes called nucleosomes are strung together like beads on a string. Protein folding then occurs in the resulting DNA-protein nucleosomes, to form a chromatin fiber. The study of the activity of chromatin is called epigenetics.

Describes the use of raman optical activity spectroscopy in yielding information on biomolecular structure. Identification of basic protein-folding patterns; Solution structure and behavior of biomolecules; Use of chiroptical spectroscopies; Identification of protein and nucleic acid components of intact viruses.

Reports on German researchers' identification of a large group of natural protein substrates of the bacterial chaperone GroEL. Chaperones as proteins that provide partially folded proteins from aggregating; Possible explanation why some proteins need assistance to fold properly.

The article focuses on application of ultra-high performance size-exclusion chromatography (UHP-SEC) by Wyatt Technology for at-line process monitoring (ALPM) of protein aggregation. Topics discussed include addition of multi-angle light scattering (MALS) analysis to UHP-SEC; use of UHP-SEC with dynamic light scattering (DLS) to monitor antibody samples; and unfavorable result of combined MALS, DLS, to UHP-SEC for species identification and conformation due to applied stress.

The article focuses on the use of nuclear magnetic resonance spectroscopy (NMR) to track protein folding. It discusses the apparatus made by Philip Anfinrud, Ad Bax for researching protein folding, the folding in regulatory protein ubiquitin, researching on atomic resolution structures into protein aggregation and fibril formation. It also talks about the impact of pressure on NMR.

The article discusses the achievements of chemistry professor Jeffery W. Kelly, recipient of Ralph F. Hirschmann Award in Peptide Chemistry. Kelly contributed to understanding the chemical basis of the folding of protein beta-sheet structures. He was born in Medina, New York and earned a degree in chemistry at the State University of New York, Fredonia. One of his previous awards include the 2008 American Peptide Society Vincent du Vigneaud Award.

The article offers updates for analytical chemistry. Scientists still developing a method that enable them to watch proteins folding that too fast to capture. Redwood Toxicology Laboratory has developed a urine test based in laboratory for designer stimulant drugs. Dionex Corp. is planning to collaborate with the Environmental Protection Agency (EPA) Office of Ground Water and Drinking Water in Cincinnati, Ohio for determination of Hexavalent chromium.

The article discusses the study conducted by Yaakov Levy and Tzachi Hagai of the Weizmann Institute of Science in Israel regarding the effect of ubiquitin on protein folding. According to the study, ubiquitin helps the degradation process in a proteasome by modifying the thermal stability of a protein and thereby helping the protein to unfold near the ubiquitin-binding site. Levy and Hagai note that the result might be significant to other cellular processes regulated by a polypeptide.

The article offers information on the method by which Michael T. Woodside of the University of Alberta and coworkers have observed and measured biomolecular folding transition paths by direct experiment. Topics discussed iclude biomolecules and DNA take certain path that take them from a disordered state to a folded state, and use of used optical tweezers and force spectroscopy to observe the microscopic diffusive motions of a DNA hairpin and a prion protein dimer.

The article discusses a study on speedy monitoring of chemical reactions presented by researchers Evan R. Williams and Daniel N. Mortensen at the American Chemical Society (ACS) national meeting in San Diego, California, in March 2016. The researchers combined ultrafast mixing and mass spectrometry to speed up monitoring. They also identified the extent of the protein folding reaction.

The article presents techniques on protein folding. Hongbin Li and Qing Peng of the University of British Columbia use two proteins as guest and host and fluorescent trytophan measures the folding of host protein. Host protein folds first for it has kinetic advantage while the guest protein also starts to fold for it is stable then sets off the unfolding of host protein. Meanwhile James U. Bowie of the University of California uses biotin and streptavidin to control folding of proteins.

The article reports that a European group has able to structurally analyze a nascent protein chain while it was still being created. The study reveals that a baby protein can fold at least partially into its native three-dimensional form while it is still attached to its parent ribosome. It could lead to a more detailed explanation of the mechanism by which molecular chaperones promote protein folding and to strategies to prevent protein misfolding, which can cause neurodegenerative diseases.

The article reports on the applications of Raman spectroscopy in biochemistry and catalysis and the commercialization of ultraviolet (UV)-Raman instrumentation, as discussed at the 2007 Pittsburgh Conference on Analytical Chemistry and Applied Spectroscopy in Chicago, Illinois. There is a need to understand how proteins fold into their native states, which is currently considered to be the single most important issue in biology. UV-Raman data from proteins and peptides were analyzed.

The article provides information about the 2007 American Chemical Society National Award Winners. The Ralph. F. Hirschmann Award in Peptide Chemistry is given to Samuel H. Gellman, professor of chemistry and biochemistry at the University of Wisconsin, Madison, for his research on nonnatural peptides and on protein folding. His research has added new dimension to peptide science as well as contributions to secondary protein structure.

Discusses the re-evaluation of the relationship of protein structure to folding mechanism and rate. Folding rate and folding speed of VlsE; Implications of the discovery that a protein as large as VlsE folds by a kinetic two mechanism for theoretical models of the folding process; Development of an equation for absolute contract order that attempts to better predict folding rates for a wide range of proteins. INSET: ENERGY LAYER CAKE..

The article reports on the development of a triosephosphate isomerase-barrel (TIM-barrel) protein fold in enzymes. It mentions its creation by researchers led by Birte Hörte of the Max Planck Institute for Developmental Biology as well as Po-Ssu Huang and David Baker of the University of Washington in Seattle. It also notes their utilization of design principles from the Rosetta protein modeling program.

In this application note, a UV LED and a high performance modular spectrometer were used together to measure the intrinsic fluorescence of the protein lysozyme in different conformational states. The objective was to demonstrate the power of modular spectroscopy for measuring inherent protein fluorescence as a means to monitor changes in the folded state of proteins. [ABSTRACT FROM AUTHOR]

Reports on the selection of Peter S. Kim as the recipient of the 1994 Eli Lilly Award of the American Chemical Society Division of Biological Chemistry. Kim's work in the field of protein folding; Educational background and career background.

The article focuses on a research by biochemist Michael S. Kay and colleagues at the University of Utah School of Medicine, related to folding of natural chaperone protein GroEL, published in the periodical "Proceedings of National Academy of Sciences" in 2014. It discusses benefits of methods for synthesizing mirror image proteins for generating larger versions of proteins and use of recombinant GroEL/ES to fold a mirror-image version of 4-hydroxy-tetrahydrodipicolinate synthase (DapA).

In this application note, a UV LED and a high performance modular spectrometer were used to measure intrinsic fluorescence for the protein lysozyme in different conformational states. The objective was to demonstrate the power of modular spectroscopy for measuring inherent protein fluorescence to monitor changes in protein folding state. [ABSTRACT FROM AUTHOR]

The article focuses on a study by researcher Simon Scheuring et al. in the journal "Science" in 2013 related to the development of the high-speed force spectroscopy. It informs that the spectroscopy speeds up studies related to protein-unfolding based on simulations and experiments. It mentions that faster analysis of proteins reduces atomic force microscopy (AFM) cantilever that pulls proteins attached to the cantilever when it is deflected and presents views of researcher Klaus Schulten.

The article discusses a research where a technique for producing novel protein catalysts was developed. It informs that protein folds and functions can be developed at the same time by introducing new catalytic sites in it. It also informs that new rules were created for explaining the junctions between adjacent structural elements which were independent of the amino acid sequences.

The article presents information about the studies related to the simulations of green fluorescent protein (GFP) folding which was found to be in agreement with previous studies on thermodynamics and kinetics of the protein folding.

The article discusses a study by Paul Wentworth Jr. of the University of Oxford and graduate students Kanlaya Prapainop and Daniel P. Witter which found that diagnostic nanoparticles can be directed to specific cell types by exploiting the protein corona.

The article cites a report in the journal "Nature Chemical Biology" regarding the discovery of compounds that could be used to develop drugs to treat diseases caused by protein-misfolding, such as Alzheimer's disease, by researchers at Northwestern University.

The article reports on the results of two studies concerning the folding of individual proteins that were published in an issue of "Science" journal.

The article reports that a retroviral protease crystal structure that had eluded scientists for years has been solved by players of the online computer game Foldit.

The article reports that structural mimics of α-helices may be created by adding β- and y-amino acids to peptides, as indicated in the results of a study that was published in a 2011 issue of the "Journal of American Chemical Society" (JACS). It explains how chemistry professor Samuel H. Gellman and post-doc Tomohisa Sawada of the University of Wisconsin, Madison, demonstrated the approach. According to Gellman, water is the toughest solution for protein folding.

The article reports on a study which found that the size of prion aggregates affects their ability to induce further aggregation and cause illness, which could be beneficial in understanding protein-misfolding diseases.

The article reports on a study which found an ion channel called SLAC1 that helps open and close pores in the leaf epidermis. The X-ray structure of the channel, which has a unique protein fold, is said to indicate that it may be useful for breeding or engineering plants that can better survive in arid environments. A team of researchers led by biochemist Wayne A. Hendrickson University crystallized a homolog of the plant protein to crystallize the SLAC1 that is buried in the plant cell membrane.

This article focuses on a study published in "Nature Chemical Biology" which examined the potential use of a noncovalent interaction in protein folding and maintaining their three-dimensional structures. Researcher Ronald T. Raines of the University of Wisconsin, Madison points out the benefit of proline's ring structure. He explains that the interaction has been ignored due to how people tend to represent and think about protein structure. He adds that there is a need to consider quantum mechanics for this particular interaction.

The article discusses a study by Arthur G. Palmer and colleagues which found a technique for enhancing the resolution in protein nuclear magnetic resonance (NMR)spectroscopy.

This article discusses a study by chemists at Northeastern University and the University of North Carolina which examined the conformation of membrane proteins in native-like conditions.

The article reports that the lipid-transfer protein from barley helps the liquid-gas interfaces in beer foam become stable after undergoing structural changes as revealed in the study led by Alan R. Mackie of the Institute of Food Research in Colney, England. Researchers say that the changes probably because of failing to properly refold the structure allow the protein to become a good stabilizer. However, the study offers another puzzle on how protein stability influences beer foam stability.

The article reports on a study regarding the relevance of protein folding to the lifespan of organisms. The study, led by Rochelle Buffenstein and Asish Chaudhuri of the University of Texas Health Science Center in San Antonio, Texas, revealed that protein stability and integrity play important roles in the longevity of life span. The method used by the researchers with the study is also discussed.

The article focuses on the study regarding the capability of enzymes to select right metal ion. Studies show that cells can ensure the enzyme picks the right metal ion by controlling which cellular compartment the protein is folding in. Cells know and can easily locate the right metal in the protein by controlling the position of nascent protein folds. Only the manganese-containing protein is allowed to fold in, since manganese has trace metals that are important for the function of enzymes.

The article discusses how researchers at Scripps Research Institute have devised a method that sufficiently improves the folding of mutant proteins to restore their function. The research team carried out the work with cells cultures form Tay-Sachs and Gaucher's disease patients. The researchers first determined that compounds such as celastrol improve the folding and function of mutant proteins in the cells.