NMR spectroscopic and theoretical analysis of a spontaneously formed Lys-Asp isopeptide bond

Robert Mark Hagan, Ragnar Bjornsson, Stephen McMahon, B Schomburg, V Braithwaite, Michael Buehl, Jim Naismith, Uli Schwarz-Linek

Research output: Contribution to journalArticlepeer-review

63 Citations (Scopus)

Abstract

One bond makes all the difference: Three suitably positioned amino acid side chains (see picture) and a hydrophobic environment are all that is required for an amidation reaction with remarkable consequences. An emerging central building block of bacterial surface proteins owes its stability to a spontaneously formed isopeptide bond. The impact of this bond on protein structure and dynamics and the mechanism of its formation are scrutinized in detail.

Original languageEnglish
Pages (from-to)8421-8425
Number of pages5
JournalAngewandte Chemie International Edition
Volume49
Issue number45
Early online date28 Sept 2010
DOIs
Publication statusPublished - Nov 2010

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