Characterizing Active Site Conformational Heterogeneity along the Trajectory of an Enzymatic Phosphoryl Transfer Reaction-Reference-Cited by-同舟云学术

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Characterizing Active Site Conformational Heterogeneity along the Trajectory of an Enzymatic Phosphoryl Transfer Reaction

Published:2016-08-18 Issue:38 Volume:55 Page:11533-11537
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angew. Chem. Int. Ed.

Author:

Zeymer Cathleen¹,Werbeck Nicolas D.²,Zimmermann Sabine¹,Reinstein Jochen¹,Hansen D. Flemming²^ORCID

Affiliation:

1. Department of Biomolecular Mechanisms; Max Planck Institute for Medical Research; Jahnstrasse 29 69120 Heidelberg Germany

2. Division of Biosciences; Institute of Structural and Molecular Biology; University College London; Gower Street London WC1E 6BT UK

Funder

BBSRC

Max Planck Society

Publisher

Wiley

Subject

General Chemistry,Catalysis

Reference33 articles.

1. Transition State Analogues for Enzyme Catalysis

2. Enzymatic Transition States, Transition-State Analogs, Dynamics, Thermodynamics, and Lifetimes

3. At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis?

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4. Mechanistic Basis for a Connection between the Catalytic Step and Slow Opening Dynamics of Adenylate Kinase;Journal of Chemical Information and Modeling;2023-02-21

5. Protein dynamics: The future is bright and complicated!;Structural Dynamics;2023-01

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