The Atomistic Mechanism of Conformational Transition of Adenylate Kinase Investigated by Lorentzian Structure-Based Potential-Reference-Cited by-同舟云学术

The Atomistic Mechanism of Conformational Transition of Adenylate Kinase Investigated by Lorentzian Structure-Based Potential

Published:2015-06-24 Issue:7 Volume:11 Page:3211-3224
ISSN:1549-9618
Container-title:Journal of Chemical Theory and Computation
language:en
Short-container-title:J. Chem. Theory Comput.

Author:

Lee Juyong¹²,Joo Keehyoung³⁴,Brooks Bernard R.²,Lee Jooyoung¹³

Affiliation:

1. School of Computational Sciences, Korea Institute for Advanced Study, Dongdaemun-gu, Seoul 130-722, Korea

2. Laboratory of Computational Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20852, United States

3. Center for In Silico Protein Science, Korea Institute for Advanced Study, Dongdaemun-gu, Seoul 130-722, Korea

4. Center for Advanced Computation, Korea Institute for Advanced Study, Dongdaemun-gu, Seoul 130-722, Korea

Funder

National Research Foundation of Korea

Publisher

American Chemical Society (ACS)

Subject

Physical and Theoretical Chemistry,Computer Science Applications

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jctc.5b00268

Reference75 articles.

1. The Way Things Move: Looking Under the Hood of Molecular Motor Proteins

2. Crystal Structure of the Dynein Motor Domain

3. Allosteric regulation and catalysis emerge via a common route

4. Structural Rearrangements Underlying K + -Channel Activation Gating

5. Intrinsic motions along an enzymatic reaction trajectory

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