Relationship between Side Chain Structure and 14-Helix Stability of β3-Peptides in Water
نویسندگان
چکیده
منابع مشابه
Relationship between side chain structure and 14-helix stability of beta3-peptides in water.
Folded polymers are used in Nature for virtually every vital process. Nonnatural folded polymers, or foldamers, have the potential for similar versatility, and the design and refinement of such molecules is of considerable current interest. Here we report a complete and systematic analysis of the relationship between side chain structure and the 14-helicity of a well-studied class of foldamers,...
متن کاملPositional screening and NMR structure determination of side-chain-to-side-chain cyclized β3-peptides.
Many β-peptides fold in a 14-helical secondary structure in organic solvents, but similar 14-helix formation in water requires additional stabilizing elements. Especially the 14-helix stabilization of short β-peptides in aqueous solution is critical, due to the limited freedom for incorporating stabilizing elements. Here we show how a single lactam bridge, connecting two β-amino acid side-chain...
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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 ...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2005
ISSN: 0002-7863,1520-5126
DOI: 10.1021/ja0459375