1. Relationship between Salt-Bridge Identity and 14-Helix Stability of β3-Peptides in Aqueous Buffer
- Author
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Michael E. Hodsdon, James D. Lear, Danielle A. Guarracino, Alanna Schepartz, Tereece N. Banks, and HyoJin R. Chiang
- Subjects
Models, Molecular ,Molecular Structure ,Protein Conformation ,Chemistry ,Organic Chemistry ,Water ,Buffers ,Salt bridge (protein and supramolecular) ,Ligand (biochemistry) ,Biochemistry ,Protein Structure, Secondary ,Structure-Activity Relationship ,Crystallography ,Aqueous buffer ,Helix ,Physical and Theoretical Chemistry ,Peptides - Abstract
We report a systematic analysis of the relationship between salt bridge composition and 14-helix structure within a family of model beta-peptides in aqueous buffer. We find an inverse relationship between side-chain length and the extent of 14-helix structure as judged by CD. Introduction of a stabilizing salt bridge pair within a previously reported beta-peptide ligand for hDM2 led to changes in structure that were detectable by NMR.
- Published
- 2006
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