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In Vivo Screening Identifies a Highly Folded β‐Hairpin Peptide with a Structured Extension
Author(s) -
Cheng Zihao,
Miskolzie Mark,
Campbell Robert E.
Publication year - 2007
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200600565
Subject(s) - haystack , in vivo , peptide , computational biology , chemistry , förster resonance energy transfer , extension (predicate logic) , small hairpin rna , biophysics , nanotechnology , biochemistry , biology , materials science , physics , computer science , genetics , fluorescence , rna , gene , quantum mechanics , world wide web , programming language
Like finding a hairpin in the haystack . We have used an in vivo FRET‐based screening method to identify highly folded β‐hairpin peptides in large libraries. An NMR structure reveals that a cross‐strand cation–π interaction helps stabilize the most highly folded β‐hairpin.
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