Journal ArticleDOI
Cold denaturation of proteins.
TLDR
In this article, the authors summarized all experimental facts concerning the cold denaturation of single-domain, multi-domain and multimeric globular proteins in aqueous solutions with and without urea and guanidine hydrochloride.Abstract:
This article summarizes all experimental facts concerning the cold denaturation of single-domain, multi-domain, and multimeric globular proteins in aqueous solutions with and without urea and guanidine hydrochloride. The facts obtained by various experimental techniques are analyzed thermodynamically and it is shown that the cold denaturation is a general phenomenon caused by the very specific and strongly termperature-dependent interaction of protein nonpolar groups with water. Hydration of these groups, in contrast to expectations, is favorable thermodynamically, i.e., the Gibbs energy of hydration is negative and increases in magnitude at a temperature decrease. As a result, the polypeptide chain, tightly packed in a compact native structure, unfolds at a sufficiently low temperature, exposing internal nonpolar groups to water. The reev-aluation of the hydration effect on the base of direct calorimetric studies of protein denaturation and of transfer of non-polar compounds into water leads to r...read more
Citations
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Journal ArticleDOI
Physical Stability of Proteins in Aqueous Solution: Mechanism and Driving Forces in Nonnative Protein Aggregation
TL;DR: The purpose of the current review is to provide a fundamental understanding of the mechanisms by which proteins aggregate and by which varying solution conditions, such as temperature, pH, salt type, salt concentration, cosolutes, preservatives, and surfactants, affect this process.
Book ChapterDOI
Energetics of protein structure.
TL;DR: This chapter summarizes the experimental information on protein energetics and investigates the correlation between thermodynamic and structural characteristics of protein, including the water-ASA of various groups in the native and unfolded states, the number of hydrogen bonds, and the extent of van der Waals contacts in thenative state.
Journal ArticleDOI
Stability of Protein Pharmaceuticals: An Update
TL;DR: This review summarizes the advances that have been made since then regarding protein stabilization and formulation and discusses the current understanding of chemical and physical instability.
Journal ArticleDOI
Design of freeze-drying processes for pharmaceuticals: practical advice.
Xiaolin Tang,Michael J. Pikal +1 more
TL;DR: It is the thesis that design of an “optimized” freeze-drying process is not particularly difficult for most products, as long as some simple rules based on well-accepted scientific principles are followed.
Journal ArticleDOI
Physical Chemistry of Biological Free Energy Transduction As Demonstrated by Elastic Protein-Based Polymers†
TL;DR: This article presents a general mechanism for protein folding and function and demonstrates the mechanism by designing model proteins capable of performing many of the energy conversions that sustain life and by designing diverse biomolecular machines and materials with promising applications for society.
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.
Journal ArticleDOI
Free Volume and Entropy in Condensed Systems III. Entropy in Binary Liquid Mixtures; Partial Molal Entropy in Dilute Solutions; Structure and Thermodynamics in Aqueous Electrolytes
Henry S. Frank,Marjorie W. Evans +1 more
TL;DR: The first and second papers in this series, which make it possible to interpret entropy data in terms of a physical picture, are applied to binary solutions, and equations are derived relating energy and volume changes when a solution is formed to the entropy change for the process as discussed by the authors.
Book ChapterDOI
Stability of Proteins Small Globular Proteins
TL;DR: The chapter discusses the stability of proteins and presents the results obtained on small compact globular proteins, which represent one single cooperative system, and the temperature-induced changes in protein, denaturational and predenaturational changes inprotein, thermodynamics of protein unfolding, and thermodynamic properties of protein.
Journal ArticleDOI
Ion-solvent interaction. Structural aspects of ion-solvent interaction in aqueous solutions: a suggested picture of water structure
Henry S. Frank,Wen-Yang Wen +1 more
TL;DR: In this paper, a new picture of water as consisting of flickering clusters of hydrogen-bonded molecules is presented, in which the cooperative nature of cluster formation and relaxation is related to the partially covalent character which is postulated for the hydrogen bond.