Projects per year
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 language | English |
---|---|
Pages (from-to) | 8421-8425 |
Number of pages | 5 |
Journal | Angewandte Chemie International Edition |
Volume | 49 |
Issue number | 45 |
Early online date | 28 Sept 2010 |
DOIs | |
Publication status | Published - Nov 2010 |
Fingerprint
Dive into the research topics of 'NMR spectroscopic and theoretical analysis of a spontaneously formed Lys-Asp isopeptide bond'. Together they form a unique fingerprint.Projects
- 2 Finished
-
Carb Export: Bacteria Ref: 081862/Z/06/Z: Carbohydrate export in bacteria
Naismith, J. (PI) & Ingledew, W. J. (CoI)
1/10/07 → 31/01/14
Project: Standard
-