Literature DB >> 241856

The heat-unfolded state of ribonuclease A is an equilibrium mixture of fast and slow refolding species.

J R Garel, R L Baldwin.   

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Year:  1975        PMID： 241856     DOI： 10.1016/0022-2836(75)90325-3

Source DB:  PubMed          Journal:  J Mol Biol        ISSN： 0022-2836            Impact factor:   5.469


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  6 in total

1.  Unfolding and refolding occur much faster for a proline-free proteins than for most proline-containing proteins.

Authors:  J F Brandts; M Brennan
Journal:  Proc Natl Acad Sci U S A       Date:  1977-10       Impact factor: 11.205

2.  Role of proline isomerization in folding of ribonuclease A at low temperatures.

Authors:  K H Cook; F X Schmid; R L Baldwin
Journal:  Proc Natl Acad Sci U S A       Date:  1979-12       Impact factor: 11.205

3.  Regeneration of RNase A from the reduced protein: models of regeneration pathways.

Authors:  Y Konishi; T Ooi; H A Scheraga
Journal:  Proc Natl Acad Sci U S A       Date:  1982-09       Impact factor: 11.205

4.  Acid catalysis of the formation of the slow-folding species of RNase A: evidence that the reaction is proline isomerization.

Authors:  F X Schmid; R L Baldwin
Journal:  Proc Natl Acad Sci U S A       Date:  1978-10       Impact factor: 11.205

5.  Evidence for involvement of proline cis-trans isomerization in the slow unfolding reaction of RNase A.

Authors:  J R Garel
Journal:  Proc Natl Acad Sci U S A       Date:  1980-02       Impact factor: 11.205

6.  Guanidine-unfolded state of ribonuclease A contains both fast- and slow-refolding species.

Authors:  J R Garel; B T Nall; R L Baldwin
Journal:  Proc Natl Acad Sci U S A       Date:  1976-06       Impact factor: 11.205
  6 in total

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