The differences in the microenvironment of the two tryptophan residues of the glutamine-binding protein fromEscherichia coli shed light on the binding properties and the structural dynamics of the protein-Reference-Cited by-同舟云学术

The differences in the microenvironment of the two tryptophan residues of the glutamine-binding protein fromEscherichia coli shed light on the binding properties and the structural dynamics of the protein

Published:2008 Issue:2 Volume:71 Page:743-750
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

D'Auria Sabato,Staiano Maria,Varriale Antonio,Gonnelli Margherita,Marabotti Anna,Rossi Mose',Strambini Giovanni B.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference36 articles.

1. Cloning and complete nucleotide sequence of the Escherichia coli glutamine permease operon (glnHPQ)

2. A Binding Protein for Glutamine and Its Relation to Active Transport in Escherichia coli

3. The Crystal Structure of Glutamine-binding Protein fromEscherichia coli

4. ABC Transporters: From Microorganisms to Man

5. Bacterial Periplasmic Binding Protein Tertiary Structures

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