Uncovering the Molecular Interactions in the Catalytic Loop That Modulate the Conformational Dynamics in Protein Tyrosine Phosphatase 1B-Reference-Cited by-同舟云学术

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Uncovering the Molecular Interactions in the Catalytic Loop That Modulate the Conformational Dynamics in Protein Tyrosine Phosphatase 1B

Published:2019-07-24 Issue:32 Volume:141 Page:12634-12647
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Cui Danica S.¹,Lipchock James Michael²,Brookner Dennis³,Loria J. Patrick¹³^ORCID

Affiliation:

1. Department of Chemistry, Yale University, New Haven, Connecticut 06511, United States

2. Department of Chemistry, Washington College, Chestertpwm, Maryland 21620, United States

3. Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511, United States

Funder

Division of Molecular and Cellular Biosciences

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.9b04470

Reference71 articles.

1. A Proficient Enzyme

2. Enzyme catalysis: not different, just better

3. The role of dynamic conformational ensembles in biomolecular recognition

4. The Energy Landscapes and Motions of Proteins

5. Dynamical Contributions to Enzyme Catalysis: Critical Tests of A Popular Hypothesis

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