Shifting the Equilibrium between the Encounter State and the Specific Form of a Protein Complex by Interfacial Point Mutations-Reference-Cited by-同舟云学术

Shifting the Equilibrium between the Encounter State and the Specific Form of a Protein Complex by Interfacial Point Mutations

Published:2010-07-30 Issue:33 Volume:132 Page:11487-11495
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Volkov Alexander N.¹,Bashir Qamar¹,Worrall Jonathan A. R.¹,Ullmann G. Matthias¹,Ubbink Marcellus¹

Affiliation:

1. Leiden Institute of Chemistry, Leiden University, Gorlaeus Laboratories, P.O. Box 9502, 2300 RA, Leiden, The Netherlands, and Structural Biology/Bioinformatics, University of Bayreuth, Universitätsstr. 30, BGI, 95447 Bayreuth, Germany

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja100867c

Reference62 articles.

1. Close Encounters of the Transient Kind: Protein Interactions in the Photosynthetic Redox Chain Investigated by NMR Spectroscopy

2. Fundamental Aspects of Protein−Protein Association Kinetics

3. Studies on Cytochrome c Peroxidase

4. Tryptophan-191 .fwdarw. phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation

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