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