Literature DB >> 5410853

Kinetics of folding of staphylococcal nuclease.

A N Schechter, R F Chen, C B Anfinsen.   

Abstract

Staplhylococcal nuclease undergoes a reversible structural transition between (p)h3 and 4 which be mesured by changes in tryptoham fluorescence. A stopped-flow spectrofluorometer was used to study the kinetics renaturation of nuclease from the acidified form on neutralization, the refolding is fast and the data can be described as a sequence of two first-order processes with half times of about 55 and 350 milliseconds, respectively.

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Year:  1970        PMID： 5410853     DOI： 10.1126/science.167.3919.886

Source DB:  PubMed          Journal:  Science        ISSN： 0036-8075            Impact factor:   47.728


  11 in total

Review 1.  Early events in protein folding explored by rapid mixing methods.

Authors:  Heinrich Roder; Kosuke Maki; Hong Cheng
Journal:  Chem Rev       Date:  2006-05       Impact factor: 60.622

2.  Inhibitor binding increases the mechanical stability of staphylococcal nuclease.

Authors:  Chien-Chung Wang; Tian-Yow Tsong; Yau-Heiu Hsu; Piotr E Marszalek
Journal:  Biophys J       Date:  2011-02-16       Impact factor: 4.033

Review 3.  Staphylococcal nuclease reviewed: a prototypic study in contemporary enzymology. IV. The nuclease as a model for protein folding.

Authors:  P W Tucker; E E Hazen; F A Cotton
Journal:  Mol Cell Biochem       Date:  1979-02-09       Impact factor: 3.396

4.  The mechanism of folding of globular proteins. Equilibria and kinetics of conformational transitions of penicillinase from Staphylococcus aureus involving a state of intermediate conformation.

Authors:  B Robson; R H Pain
Journal:  Biochem J       Date:  1976-05-01       Impact factor: 3.857

5.  The kinetic basis for the stabilization of staphylococcal nuclease by xylose.

Authors:  K J Frye; C A Royer
Journal:  Protein Sci       Date:  1997-04       Impact factor: 6.725

6.  Folding of staphylococcal nuclease: magnetic resonance and fluorescence studies of individual residues.

Authors:  H F Epstein; A N Schechter; J S Cohen
Journal:  Proc Natl Acad Sci U S A       Date:  1971-09       Impact factor: 11.205

7.  Nonuniform chain collapse during early stages of staphylococcal nuclease folding detected by fluorescence resonance energy transfer and ultrarapid mixing methods.

Authors:  Takuya Mizukami; Ming Xu; Hong Cheng; Heinrich Roder; Kosuke Maki
Journal:  Protein Sci       Date:  2013-08-19       Impact factor: 6.725

8.  The sequential unfolding of ribonuclease A: detection of a fast initial phase in the kinetics of unfolding.

Authors:  T Y Tsong; R L Baldwin; E L Elson
Journal:  Proc Natl Acad Sci U S A       Date:  1971-11       Impact factor: 11.205

9.  Least activation path for protein folding: investigation of staphylococcal nuclease folding by stopped-flow circular dichroism.

Authors:  Z D Su; M T Arooz; H M Chen; C J Gross; T Y Tsong
Journal:  Proc Natl Acad Sci U S A       Date:  1996-03-19       Impact factor: 11.205

10.  The Role of Endoplasmic Reticulum Chaperones in Protein Folding and Quality Control.

Authors:  Benjamin M Adams; Nathan P Canniff; Kevin P Guay; Daniel N Hebert
Journal:  Prog Mol Subcell Biol       Date:  2021
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