NMR characterization of an engineered domain fusion between maltose binding protein and TEM1 β-lactamase provides insight into its structure and allosteric mechanism-Reference-Cited by-同舟云学术

NMR characterization of an engineered domain fusion between maltose binding protein and TEM1 β-lactamase provides insight into its structure and allosteric mechanism

Published:2009-11-24 Issue:6 Volume:78 Page:1423-1430
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Wright Chapman M.,Majumdar Ananya,Tolman Joel R.,Ostermeier Marc

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/prot.22657/fullpdf

Reference21 articles.

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4. Directed evolution of protein switches and their application to the creation of ligand-binding proteins;Guntas;Proc Natl Acad Sci USA,2005

5. Purification and properties of thiol beta-lactamase. A mutant of pbr322 beta-lactamase in which the active site serine has been replaced with cysteine;Sigal;J Biol Chem,1984

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