Water and globular proteins
TLDR
In this article, dynamic, thermodynamic and structural studies of the hydration of globular proteins indicate how the macromolecule-water interface can influence folding, enzymatic activity and other biological properties.About:
This article is published in Trends in Biochemical Sciences.The article was published on 1983-01-01 and is currently open access. It has received 412 citations till now. The article focuses on the topics: Globular protein & Folding (chemistry).read more
Citations
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Beyond water activity: recent advances based on an alternative approach to the assessment of food quality and safety
TL;DR: The effects of water, as a near-universal solvent and plasticizer, on the behavior of polymeric (as well as oligomeric and monomeric) food materials and systems, are reviewed, with emphasis on the impact of water content (in terms of increasing system mobility and eventual water "availability") on food quality, safety, stability, and technological performance.
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Effective energy function for proteins in solution.
Themis Lazaridis,Martin Karplus +1 more
TL;DR: Results reported elsewhere show that EEF1 clearly distinguishes correctly from incorrectly folded proteins, both in static energy evaluations and in molecular dynamics simulations and that unfolding pathways obtained by high‐temperature Molecular dynamics simulations agree with those obtained by explicit water simulations.
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Hydrogen exchange and structural dynamics of proteins and nucleic acids
TL;DR: Though the structures presented in crystallographic models of macromolecules appear to possess rock-like solidity, real proteins and nucleic acids are not particularly rigid.
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Enzymatic catalysis in organic media at 100 degrees C
TL;DR: Porcine pancreatic lipase catalyzes the transesterification reaction between tributyrin and various primary and secondary alcohols in a 99 percent organic medium and exhibits a high catalytic activity at that temperature.
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Enzymatic catalysis in nonaqueous solvents.
TL;DR: The rate enhancements afforded by chymotrypsin and subtilisin in the transesterification reaction in octane are of the order of 100 billion-fold; covalent modification of the active center of the enzymes by a site-specific reagent renders them catalytically inactive in organic solvents.
References
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Journal ArticleDOI
Dynamics of folded proteins
TL;DR: The dynamics of a folded globular protein have been studied by solving the equations of motion for the atoms with an empirical potential energy function and suggest that the protein interior is fluid-like in that the local atom motions have a diffusional character.
Book ChapterDOI
Hydration of Proteins and Polypeptides
Irwin D. Kuntz,W. Kauzmann +1 more
TL;DR: The chapter presents several proposals for predicting protein hydration based on the amino acid composition of the protein; however, the two main questions concerned include—whether ionic groups are more hydrated than other polar groups, and whether the amide and peptide functions are hydrated or not.
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Solvent viscosity and protein dynamics
D. Beece,L. Eisenstein,Hans Frauenfelder,D. Good,M. C. Marden,Lou Reinisch,A. H. Reynolds,Larry B. Sorensen,Kwok To Yue +8 more
TL;DR: In this article, the binding of CO to protoheme and O2 and CO to myoglobin in many different solvents was studied, and the transition rates in heme-CO are inversely proportional to the solvent viscosity and can consequently be described by the Kramers equation.
Book ChapterDOI
Energetics of Ligand Binding to Proteins
TL;DR: This chapter describes the multiple ligand binding by proteins, binding by multimer proteins, extension of the concept of ligand interaction to covalent bond exchange, cooperativity and ligand correlation, and biological specificity andligand binding.