Journal Article10.3109/10409239009090612
Cold denaturation of proteins.
1K
TL;DR: 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.
read more
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
Chat with Paper
AI Agents for this Paper
Find similar papers on Google Scholar, PubMed and Arxiv
Write a critical review of this paper
Analyze citations of this paper to find unaddressed research gaps
Citations
Evolution of Transient Receptor Potential (TRP) Ion Channels in Antarctic Fishes (Cryonotothenioidea) and Identification of Putative Thermosensors
Julia M. York,Harold H. Zakon +1 more
TL;DR: It is concluded that TRPV1a, TRPA1b, and TRPM4 are the likeliest putative thermosensors, and evidence of diversifying selection at sites across these proteins is found, putting forward hypotheses for molecular mechanisms of other cryonotothenioid adaptations.
Folding of a de novo designed native-like four-helix bundle protein.
TL;DR: The folding pathway of (α2)2 can be described by a three-state transition including a monomeric molten globule-like state, demonstrating the existence of molten-globule monomers.
Experiment-guided thermodynamic simulations on reversible two-state proteins: implications for protein thermostability.
TL;DR: Analysis of the Gibbs-Helmholtz equation has allowed us to study the interdependence of the thermodynamic parameters TG, DeltaHG and DeltaCp and their derivatives in a more rigorous way than possible by the limited experimental protein thermodynamics data available in the literature.
Thermodynamic Stability of the Transcription Regulator PaaR2 from Escherichia coli O157:H7.
Pieter De Bruyn,Pieter De Bruyn,San Hadži,San Hadži,San Hadži,Alexandra Vandervelde,Alexandra Vandervelde,Albert Konijnenberg,Albert Konijnenberg,Albert Konijnenberg,Maruša Prolič-Kalinšek,Maruša Prolič-Kalinšek,Yann G.-J. Sterckx,Yann G.-J. Sterckx,Yann G.-J. Sterckx,Frank Sobott,Frank Sobott,Jurij Lah,Laurence Van Melderen,Remy Loris,Remy Loris +20 more
TL;DR: It is demonstrated that PaaR2 mainly consists of α-helices and displays a concentration-dependent octameric build-up in solution and that this octamer contains a global shape that is significantly nonspherical.
Trehalose synthesis is induced upon exposure of Escherichia coli to cold and is essential for viability at low temperatures
TL;DR: OtsA/otsB induction and trehalose synthesis are activated during cold shock (as well as during heat shock) and play an important role in resistance of E. coli (and probably other organisms) to low temperatures.
References
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.
4.8K
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.
2.7K
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.
2.1K