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

3. Water Dynamics in the Hydration Shells of Biomolecules

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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