Premium
Cover Feature: Impact of Azidohomoalanine Incorporation on Protein Structure and Ligand Binding (ChemBioChem 23/2017)
Author(s) -
Lehner Florian,
Kudlinzki Denis,
Richter Christian,
MüllerWerkmeister Henrike M.,
Eberl Katharina B.,
Bredenbeck Jens,
Schwalbe Harald,
Silvers Robert
Publication year - 2017
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.201700603
Subject(s) - chemistry , amino acid , methionine , cover (algebra) , ligand (biochemistry) , nuclear magnetic resonance spectroscopy , feature (linguistics) , stereochemistry , crystallography , combinatorial chemistry , biochemistry , philosophy , engineering , mechanical engineering , linguistics , receptor
The cover feature picture shows the structure of the unnatural amino acid–modified PDZ3 domain, which was thoroughly investigated by NMR spectroscopy and X‐ray crystallography. Azidohomoalanine was introduced by expression in methionine auxotrophic cells to study the impact of the incorporation of an unnatural amino acid on protein structure, dynamics, and ligand binding properties. The results led to the formulation of a flexible guideline that could help researchers that study systems containing unnatural amino acids. More information can be found in the full paper by H. Schwalbe, R. Silvers, et al. on page 2340 in Issue 23, 2017 (DOI: 10.1002/cbic.201700437).