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Analysis of Peptide Secondary Structures by Photoactivatable Amino Acid Analogues
Author(s) -
Kölbel Knut,
Ihling Christian H.,
Sinz Andrea
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201205308
Subject(s) - peptide , chemistry , diazirine , intramolecular force , amino acid , mass spectrometry , combinatorial chemistry , computational biology , stereochemistry , biochemistry , chromatography , biology
Photochemical cross‐linking was applied to trap intramolecular interactions in peptides. The incorporation of diazirine‐labeled amino acid analogues in combination with high‐resolution mass spectrometry made it possible to catch reverse‐turn conformations within peptides, exactly map their self‐interacting surfaces, and discriminate between stable and transient interactions.