期刊
CHEMISTRY-A EUROPEAN JOURNAL
卷 13, 期 20, 页码 5753-5764出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.200601753
关键词
amino acids; cation-pi interactions; noncovalent interactions; peptides; protein models
资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM071589] Funding Source: NIH RePORTER
- NIGMS NIH HHS [GM 071589] Funding Source: Medline
The effects of N-methylation and chain length on a cation-pi interaction have been investigated within the context of a beta-hairpin peptide. Significant enhancement of the interaction and structural stabilization of the hairpin have been observed upon Lys methylation. Thermodynamic analysis indicates an increased entropic driving force for folding upon methylation of Lys residues. Comparison of lysine to analogues ornithine (Orn) and diami-nobutyric acid (Dab) indicates that lysine provides the strongest cation-pi interaction and also provides the most stable beta-hairpin due to a combination of side chain-side chain interactions and beta-sheet propensities. These studies have significance for the recognition of methylated lysine in histone proteins.
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