Literature DB >> 6838814

Mechanism for the unfolding and refolding of ribonuclease A. Simulations using a simple model with no structural intermediates.

L N Lin, J F Brandts.   

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Year:  1983        PMID： 6838814     DOI： 10.1021/bi00272a008

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  6 in total

1.  A carboxypeptidase Y pulse method to study the accessibility of the C-terminal end during the refolding of ribonuclease A.

Authors:  W Teschner; R Rudolph
Journal:  Biochem J       Date:  1989-06-01       Impact factor: 3.857

2.  Role of proline peptide bond isomerization in unfolding and refolding of ribonuclease.

Authors:  F X Schmid; R Grafl; A Wrba; J J Beintema
Journal:  Proc Natl Acad Sci U S A       Date:  1986-02       Impact factor: 11.205

3.  Is there a single pathway for the folding of a polypeptide chain?

Authors:  S C Harrison; R Durbin
Journal:  Proc Natl Acad Sci U S A       Date:  1985-06       Impact factor: 11.205

4.  Slow-folding kinetics of ribonuclease-A by volume change and circular dichroism: evidence for two independent reactions.

Authors:  J A Ybe; P C Kahn
Journal:  Protein Sci       Date:  1994-04       Impact factor: 6.725

5.  Kinetic circular dichroism shows that the S-peptide alpha-helix of ribonuclease S unfolds fast and refolds slowly.

Authors:  A M Labhardt
Journal:  Proc Natl Acad Sci U S A       Date:  1984-12       Impact factor: 11.205

6.  Detection of cis and trans X-Pro peptide bonds in proteins by 13C NMR: application to collagen.

Authors:  S K Sarkar; P E Young; C E Sullivan; D A Torchia
Journal:  Proc Natl Acad Sci U S A       Date:  1984-08       Impact factor: 11.205
  6 in total

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