Proton Transfer Kinetics in Histidine Side Chains Determined by pH-Dependent Multi-Nuclear NMR Relaxation-Reference-Cited by-同舟云学术

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Proton Transfer Kinetics in Histidine Side Chains Determined by pH-Dependent Multi-Nuclear NMR Relaxation

Published:2024-08-05 Issue:32 Volume:146 Page:22284-22294
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Raum Heiner N.¹,Modig Kristofer²,Akke Mikael²^ORCID,Weininger Ulrich¹^ORCID

Affiliation:

1. Institute of Physics, Biophysics, Martin-Luther-University Halle-Wittenberg, Halle (Saale) D-06120, Germany

2. Division of Biophysical Chemistry, Center for Molecular Protein Science, Department of Chemistry, Lund University, P.O. Box 124, Lund SE-22100, Sweden

Funder

Vetenskapsr?det

Deutsche Forschungsgemeinschaft

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.4c04647

Reference52 articles.

1. Determination of the tautomeric form of the imidazole ring of L-histidine in basic solution by carbon-13 magnetic resonance spectroscopy

2. Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR

3. Dynamics of Aromatic Side Chains in the Active Site of FKBP12

4. Analysis of Catalytic Residues in Enzyme Active Sites

5. Understanding the Functional Roles of Amino Acid Residues in Enzyme Catalysis

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