Journal ArticleDOI
Preferential interactions of urea with lysozyme and their linkage to protein denaturation.
Serge N. Timasheff,Guifu Xie +1 more
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TLDR
Both the stabilization and destabilization of proteins by co-solvents are controlled predominantly by preferential interactions with peptide groups newly exposed on denaturation.About:
This article is published in Biophysical Chemistry.The article was published on 2003-09-01. It has received 147 citations till now. The article focuses on the topics: Urea & Protein destabilization.read more
Citations
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Journal ArticleDOI
Cryoprotectant Toxicity: Facts, Issues, and Questions
TL;DR: This review attempts to describe what is known about CPA toxicity, theories of CPA Toxicology, and strategies to reduce CPAoxicity.
Journal ArticleDOI
Urea’s Action on Hydrophobic Interactions
TL;DR: It is shown by molecular dynamics simulations that a 7 M aqueous urea solution unfolds a chain of purely hydrophobic groups which otherwise adopts a compact structure in pure water, and that urea forms stronger attractive dispersion interactions with the protein side chains and backbone than does water and, therefore, is able to dissolve the core Hydrophobic region.
Journal ArticleDOI
Interaction of urea with amino acids: Implications for urea-induced protein denaturation
TL;DR: The results suggest that hydrophobic interactions are the dominant driving force, while hydrogen bonds between urea and the protein backbone contribute markedly to the overall energetics by avoiding unfavorable unsatisfied hydrogen bond sites on the backbone.
Journal ArticleDOI
Biotechnology applications of amino acids in protein purification and formulations.
TL;DR: This review covers various biotechnology applications of amino acids, in particular arginine, which finds much wider applications than previously anticipated in the research and development of proteins, in particularly in pharmaceutical applications.
Journal ArticleDOI
Recent Applications of Kirkwood–Buff Theory to Biological Systems
Veronica Pierce,Myungshim Kang,Mahalaxmi Aburi,Mahalaxmi Aburi,Samantha Weerasinghe,Samantha Weerasinghe,Paul E. Smith +6 more
TL;DR: The existing models of denaturation are analyzed in terms of Kirkwood–Buff theory, and the use of KB theory to interpret computer simulation data for these systems is discussed.
References
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Book ChapterDOI
Some factors in the interpretation of protein denaturation.
TL;DR: The chapter reviews that the denaturation is a process in which the spatial arrangement of the polypeptide chains within the molecule is changed from that typical of the native protein to a more disordered arrangement.
Book ChapterDOI
Protein denaturation. C. Theoretical models for the mechanism of denaturation.
TL;DR: This chapter reviews theoretical models that might be constructed and equations that may be derived from them to understand the process of protein denaturation and finds that they can be predicted semiquantitatively.
Journal ArticleDOI
Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding.
TL;DR: Denaturant m values, the dependence of the free energy of unfolding on denaturant concentration, have been collected for a large set of proteins and correlate very strongly with the amount of protein surface exposed to solvent upon unfolding.
Book ChapterDOI
Linked functions and reciprocal effects in hemoglobin: a second look.
TL;DR: In this article, the authors discuss linked functions and reciprocal effects in hemoglobin and show that not only do the linkage relations apply irrespective of whether the macromolecules undergo chemical change or polymerization, but also whether the ligands themselves associate and dissociate, possibly as macromocules.
Related Papers (5)
The molecular basis for the chemical denaturation of proteins by urea
Brian J. Bennion,Valerie Daggett +1 more