Literature DB >> 6282306

Fast- and slow-refolding forms of unfolded ribonuclease A differ in tyrosine fluorescence.

A Rehage, F X Schmid.   

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Year:  1982        PMID： 6282306     DOI： 10.1021/bi00536a006

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


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  5 in total

1.  Ultrarapid mixing experiments shed new light on the characteristics of the initial conformational ensemble during the folding of ribonuclease A.

Authors:  Ervin Welker; Kosuke Maki; M C Ramachandra Shastry; Darmawi Juminaga; Rajiv Bhat; Harold A Scheraga; Heinrich Roder
Journal:  Proc Natl Acad Sci U S A       Date:  2004-12-01       Impact factor: 11.205

2.  Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutation.

Authors:  D A Schultz; F X Schmid; R L Baldwin
Journal:  Protein Sci       Date:  1992-07       Impact factor: 6.725

3.  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

4.  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

5.  Folding pathway of guanidine-denatured disulfide-intact wild-type and mutant bovine pancreatic ribonuclease A.

Authors:  R W Dodge; J H Laity; D M Rothwarf; S Shimotakahara; H A Scheraga
Journal:  J Protein Chem       Date:  1994-05
  5 in total

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