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Relationship between Salt-Bridge Identity and 14-Helix Stability of β3-Peptides in Aqueous Buffer
- Source :
- Organic Letters. 8:807-810
- Publication Year :
- 2006
- Publisher :
- American Chemical Society (ACS), 2006.
-
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.
- 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
Subjects
Details
- ISSN :
- 15237052 and 15237060
- Volume :
- 8
- Database :
- OpenAIRE
- Journal :
- Organic Letters
- Accession number :
- edsair.doi.dedup.....c113194f536cc343eae36349e4370a72
- Full Text :
- https://doi.org/10.1021/ol0527532