Tautomeric stabilities of 4-fluorohistidine shed new light on mechanistic experiments with labeled ribonuclease A-Reference-Cited by-同舟云学术

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Tautomeric stabilities of 4-fluorohistidine shed new light on mechanistic experiments with labeled ribonuclease A

Published:2016-12 Issue: Volume:666 Page:58-61
ISSN:0009-2614
Container-title:Chemical Physics Letters
language:en
Short-container-title:Chemical Physics Letters

Author:

Kasireddy Chandana,Ellis Jonathan M.,Bann James G.,Mitchell-Koch Katie R.

Funder

NIH National Institute of General Medical Sciences

National Science Foundation

Publisher

Elsevier BV

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Reference42 articles.

1. Ribonuclease A

2. His ... Asp Catalytic Dyad of Ribonuclease A: Histidine pKa Values in the Wild-Type, D121N, and D121A Enzymes

3. Enzyme transition states from theory and experiment

4. The mechanism of rate-limiting motions in enzyme function

5. The Flexibility of a Distant Loop Modulates Active Site Motion and Product Release in Ribonuclease A

Cited by 6 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Analysis of Multiple Protein Alignments Using 3D-Structural Information on the Orientation of Amino Acid Side-Chains;Molecular Biology;2022-08

2. Newly identified C–H⋯O hydrogen bond in histidine;Physical Chemistry Chemical Physics;2022

3. Ribonuclease A;Enzyme Active Sites and their Reaction Mechanisms;2021

4. Progress in Our Understanding of 19F Chemical Shifts;Annual Reports on NMR Spectroscopy;2018

5. Evaluating electronic structure methods for accurate calculation of 19 F chemical shifts in fluorinated amino acids;Journal of Computational Chemistry;2017-08-21

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