Multinuclear magnetic resonance studies of Escherichia coli adenylate kinase in free and bound forms . Resonance assignment, secondary structure and ligand binding-Reference-Cited by-同舟云学术

Multinuclear magnetic resonance studies of Escherichia coli adenylate kinase in free and bound forms . Resonance assignment, secondary structure and ligand binding

Published:1999-09-15 Issue:3 Volume:264 Page:765-774
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:Eur J Biochem

Author:

Burlacu-Miron Simona,Gilles Anne-Marie,Popescu Aurel,Barzu Octavian,Craescu Constantin T.

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1432-1327.1999.00633.x/fullpdf

Reference36 articles.

1. Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 Å resolution

2. Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding

3. Induced-fit movements in adenylate kinases

4. Domain Closure in Adenylate Kinase

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