Peptide .alpha.-helicity in aqueous trifluoroethanol: correlations with predicted .alpha.-helicity and the secondary structure of the corresponding regions of bovine growth hormone-Reference-Cited by-同舟云学术

Peptide .alpha.-helicity in aqueous trifluoroethanol: correlations with predicted .alpha.-helicity and the secondary structure of the corresponding regions of bovine growth hormone

Published:1990-06-12 Issue:23 Volume:29 Page:5590-5596
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Lehrman S. Russ,Tuls Jody L.,Lund Marilyn

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00475a025

Reference29 articles.

1. Three-dimensional structure of a genetically engineered variant of porcine growth hormone.

2. A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A.

3. Folding of bovine growth hormone is consistent with the molten globule hypothesis

4. The kinetics of bovine growth hormone folding are consistent with a framework model.

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