Literature DB >> 15454460

Protein stiffening and entropic stabilization in the subdenaturing limit of guanidine hydrochloride.

Rajesh Kumar1, N Prakash Prabhu, M Yadaiah, Abani K Bhuyan.   

Abstract

Subdenaturing concentrations of guanidine hydrochloride (GdnHCl) stabilize proteins. For ferrocytochrome c the stabilization is detected at subglobal level with no measured change in global stability. These deductions are made by comparing observed rates of thermally driven ferrocytochrome cHCO reactions with global unfolding rates of ferrocytochrome c measured by stopped flow and NMR hydrogen exchange in the presence of a wide range of GdnHCl concentrations at pH 7, 22 degrees C. Copyright 2004 Biophysical Society

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Year:  2004        PMID: 15454460      PMCID: PMC1304684          DOI: 10.1529/biophysj.104.044701

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  20 in total

1.  Protein interactions with urea and guanidinium chloride. A calorimetric study.

Authors:  G I Makhatadze; P L Privalov
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2.  Evidence for an unfolding and refolding pathway in cytochrome c.

Authors:  Y Xu; L Mayne; S W Englander
Journal:  Nat Struct Biol       Date:  1998-09

3.  Anion binding to the ubiquitin molecule.

Authors:  G I Makhatadze; M M Lopez; J M Richardson; S T Thomas
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4.  The effect of denaturants on protein structure.

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5.  Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability.

Authors:  B Ibarra-Molero; V V Loladze; G I Makhatadze; J M Sanchez-Ruiz
Journal:  Biochemistry       Date:  1999-06-22       Impact factor: 3.162

6.  Folding of horse cytochrome c in the reduced state.

Authors:  A K Bhuyan; J B Udgaonkar
Journal:  J Mol Biol       Date:  2001-10-05       Impact factor: 5.469

7.  Stopped-flow NMR measurement of hydrogen exchange rates in reduced horse cytochrome c under strongly destabilizing conditions.

Authors:  A K Bhuyan; J B Udgaonkar
Journal:  Proteins       Date:  1998-08-01

8.  Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions.

Authors:  O D Monera; C M Kay; R S Hodges
Journal:  Protein Sci       Date:  1994-11       Impact factor: 6.725

9.  Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase.

Authors:  N A Morjana; B J McKeone; H F Gilbert
Journal:  Proc Natl Acad Sci U S A       Date:  1993-03-15       Impact factor: 11.205

10.  A structural basis for the interaction of urea with lysozyme.

Authors:  A C Pike; K R Acharya
Journal:  Protein Sci       Date:  1994-04       Impact factor: 6.725

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  7 in total

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