Enhanced Binding Affinity via Destabilization of the Unbound State: A Millisecond Hydrogen–Deuterium Exchange Study of the Interaction between p53 and a Pleckstrin Homology Domain-Reference-Cited by-同舟云学术

Enhanced Binding Affinity via Destabilization of the Unbound State: A Millisecond Hydrogen–Deuterium Exchange Study of the Interaction between p53 and a Pleckstrin Homology Domain

Published:2017-07-19 Issue:32 Volume:56 Page:4127-4133
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Zhu Shaolong¹,Khatun Rahima²,Lento Cristina¹,Sheng Yi²,Wilson Derek J.¹³^ORCID

Affiliation:

1. Department of Chemistry, York University, Toronto, Ontario, Canada M3J 1P3

2. Department of Biology, York University, Toronto, Ontario, Canada M3J 1P3

3. Centre for Research in Mass Spectrometry, York University, Toronto, Ontario, Canada M3J 1P3

Funder

Krembil Foundation

Natural Sciences and Engineering Research Council of Canada

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.7b00193

Reference34 articles.

1. Conformational changes associated with protein–protein interactions

2. Transient Protein-Protein Interactions: Structural, Functional, and Network Properties

3. Principles of protein-protein interactions.

4. Linear motifs: Evolutionary interaction switches

5. Multisite Phosphorylation and the Integration of Stress Signals at p53

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