Helical peptide and protein design.

Abstract:

:The design of dimeric coiled-coils has ultimately led to novel applications, such as self-replicating peptide systems, whereas the structural features of the less common trimeric coiled-coil continue to be elucidated. Novel topologies have been discovered in designed proteins, as exemplified by the right-handed tetrameric coiled-coil and the inverted U four-helix bundle, and a single switch of two amino acids within a protein has been shown to be sufficient to designate a new protein fold. Conformational switching from helix to sheet has been observed for designed peptides and transcription factors, whereas peptides designed from beta-amino acids have been found to adopt a helical conformation in aqueous solution.

journal_name

Curr Opin Chem Biol

authors

Micklatcher C,Chmielewski J

doi

10.1016/s1367-5931(99)00031-9

subject

Has Abstract

pub_date

1999-12-01 00:00:00

pages

724-9

issue

6

eissn

1367-5931

issn

1879-0402

pii

S1367-5931(99)00031-9

journal_volume

3

pub_type

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