Journal ArticleDOI
On the Refractive Indices of Aqueous Solutions of Urea
John R. Warren,Julius A. Gordon +1 more
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This article is published in The Journal of Physical Chemistry.The article was published on 1966-01-01. It has received 98 citations till now. The article focuses on the topics: Aqueous solution & Urea.read more
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Charge interactions can dominate the dimensions of intrinsically disordered proteins
Sonja Müller-Späth,Andrea Soranno,Verena Hirschfeld,Verena Hirschfeld,Hagen Hofmann,Stefan Rüegger,Stefan Rüegger,Luc Reymond,Luc Reymond,Daniel Nettels,Benjamin Schuler +10 more
TL;DR: This work uses single-molecule Forster resonance energy transfer to investigate the influence of charged residues on the dimensions of unfolded and intrinsically disordered proteins and finds that IDPs can exhibit a prominent expansion at low ionic strength that correlates with their net charge.
Journal ArticleDOI
Estimation of the free energy of stabilization of ribonuclease A, lysozyme, alpha-lactalbumin, and myoglobin.
Faizan Ahmad,C C Bigelow +1 more
TL;DR: The denaturation of ribonuclease A, lysozyme alpha-lactalbumin, and myoglobin by urea, Guanidine hydrochloride, and guanidine thiocyanate has been followed with the use of difference spectral measurements and the free energy of stabilization (delta GH2OD) has been determined.
Journal ArticleDOI
Preferential interactions of urea with lysozyme and their linkage to protein denaturation.
Serge N. Timasheff,Guifu Xie +1 more
TL;DR: Both the stabilization and destabilization of proteins by co-solvents are controlled predominantly by preferential interactions with peptide groups newly exposed on denaturation.
Journal ArticleDOI
Stability of casein micelles cross-linked by transglutaminase
TL;DR: The amount of light scattered by casein micelles in noncross-linked milk was reduced by >95% on complete disruption of hydrophobic interactions or complete solubilization of MCP; treatment of milk with TGase increased the stability of casein mouselles against disruption by all methods studied and stability increased progressively with incubation time.
Journal ArticleDOI
Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation.
TL;DR: A comparison of the effects of various potassium salts revealed that anions were chiefly responsible in stabilizing HSA, suggesting that preferential binding of anions to HSA rather than hydration, was primarily responsible for stabilization.
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Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants.
Marcelo M. Santoro,D. W. Bolen +1 more