Physical reasons for secondary structure stability: α-Helices in short peptides
Author:
Publisher
Wiley
Subject
Molecular Biology,Biochemistry,Structural Biology
Reference54 articles.
1. A competing salt-bridge suppresses helix formation by the isolated C-peptide carboxylate of ribonuclease A
2. A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A.
3. A helix stop signal in the isolated S-peptide of ribonuclease A
4. Nature of the charged-group effect on the stability of the C-peptide helix.
5. The design and production of semisynthetic ribonucleases with increased thermostability by incorporation of S-peptide analogues with enhanced helical stability
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