Fast Microsecond Dynamics of the Protein–Water Network in the Active Site of Human Carbonic Anhydrase II Studied by Solid-State NMR Spectroscopy-Reference-Cited by-同舟云学术

Fast Microsecond Dynamics of the Protein–Water Network in the Active Site of Human Carbonic Anhydrase II Studied by Solid-State NMR Spectroscopy

Published:2019-10-24 Issue:49 Volume:141 Page:19276-19288
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Singh Himanshu¹²^ORCID,Vasa Suresh K.¹²^ORCID,Jangra Harish²,Rovó Petra²^ORCID,Päslack Christopher³,Das Chandan K.³,Zipse Hendrik²^ORCID,Schäfer Lars V.³^ORCID,Linser Rasmus¹²^ORCID

Affiliation:

1. Faculty of Chemistry and Chemical Biology, Technical University Dortmund, Otto-Hahn-Straße 4a, 44227 Dortmund, Germany

2. Department of Chemistry, Ludwig-Maximilians-University Munich, Butenandtstraße 5-13, 81377 Munich, Germany

3. Theoretical Chemistry, Ruhr University Bochum, Universitätsstraße 150, 44801 Bochum, Germany

Funder

Deutsche Forschungsgemeinschaft

Verband der Chemischen Industrie

Excellence Clusters CiPS-M and RESOLV

Center for Nanoscience

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

http://pubs.acs.org/doi/pdf/10.1021/jacs.9b05311

Reference88 articles.

1. Water Determines the Structure and Dynamics of Proteins

2. Protein folding is slaved to solvent motions

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4. Kinetic and Structural Insights into the Mechanism of Binding of Sulfonamides to Human Carbonic Anhydrase by Computational and Experimental Studies

5. Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes

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