A Billion-fold Range in Acidity for the Solvent-Exposed Amides of Pyrococcus furiosus Rubredoxin-Reference-Cited by-同舟云学术

A Billion-fold Range in Acidity for the Solvent-Exposed Amides of Pyrococcus furiosus Rubredoxin

Published:2008-05-15 Issue:23 Volume:47 Page:6178-6188
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Anderson Janet S.¹,Hernández Griselda¹,LeMaster David M.¹

Affiliation:

1. Department of Chemistry, Union College, Schenectady, New York 12308, and Wadsworth Center, New York State Department of Health, and Department of Biomedical Sciences, School of Public Health, University at Albany-State University of New York, Empire State Plaza, Albany, New York 12201

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi800284y

Reference55 articles.

1. Measuring the Conformational Stability of a Protein by Hydrogen Exchange

2. The hydrogen exchange core and protein folding

3. Protein stability parameters measured by hydrogen exchange

4. Crystal structure of rubredoxin from Pyrococcus furiosus at 0.95 Å resolution, and the structures of N-terminal methionine and formylmethionine variants of Pf Rd. Contributions of N-terminal interactions to thermostability

5. The interpretation of protein structures: Estimation of static accessibility

Cited by 35 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. Temperature-dependent iron motion in extremophile rubredoxins – no need for ‘corresponding states’;Scientific Reports;2024-05-28

2. Temperature-Dependent Iron Motion in Extremophile Rubredoxins – No Need for ‘Corresponding States’;2023-12-27

3. Transient conformations in the unliganded FK506 binding domain of FKBP51 correspond to two distinct inhibitor-bound states;Journal of Biological Chemistry;2023-09

4. Computational Modeling of Molecular Structures Guided by Hydrogen-Exchange Data;Journal of the American Society for Mass Spectrometry;2022-01-25

5. Prediction and Validation of a Protein’s Free Energy Surface Using Hydrogen Exchange and (Importantly) Its Denaturant Dependence;Journal of Chemical Theory and Computation;2021-12-22