Literature DB >> 241857

A physical difference between the fast- and slow-refolding forms of nitrotyrosyl ribonuclease A: the pK values of the nitrotyrosyl groups.

J R Garel, R L Baldwin.   

Abstract

Mesh：

Substances：

Year:  1975        PMID： 241857     DOI： 10.1016/0022-2836(75)90326-5

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


× No keyword cloud information.
  6 in total

1.  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

2.  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

3.  Transient conformational states in proteins followed by differential labeling.

Authors:  C Ghélis
Journal:  Biophys J       Date:  1980-10       Impact factor: 4.033

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.  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

6.  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 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.