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
Temperature, Pressure, and Concentration Derivatives of Nonpolar Gas Hydration: Impact on the Heat Capacity, Temperature of Maximum Density, and Speed of Sound of Aqueous Mixtures
TL;DR: Many distinct phenomena associated with the hydrophobic effect can be captured within a single thermodynamically consistent correlation for solute hydration free energies.
10
Ice and Its Formation
Amir Haji-Akbari
- 01 Jan 2020
TL;DR: The structure of ice and its polymorphism, the thermodynamics and kinetics of ice formation from pure water and aqueous solutions, and the processes that result in the formation of amorphous glassy water will be discussed in detail.
10
The Protein Unfolded State: One, No One and One Hundred Thousand
TL;DR: In this paper , a review examines recent data on the characteristics of the unfolded states emerging from experiments under different conditions, focusing specific attention to the level of compaction of the unfolding species.
10
Mechanism for proteins destabilization at low temperatures
TL;DR: The correct understanding of this process may be useful to artificially implement activation and inactivation of proteins at room temperatures with direct applications into the word of nanobiotechnology machinery.
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