Critical Evaluation of the Two-State Model Describing the Equilibrium Unfolding of the PI3K SH3 Domain by Time-Resolved Fluorescence Resonance Energy Transfer-Reference-Cited by-同舟云学术

Critical Evaluation of the Two-State Model Describing the Equilibrium Unfolding of the PI3K SH3 Domain by Time-Resolved Fluorescence Resonance Energy Transfer

Published:2013-12-19 Issue:52 Volume:52 Page:9482-9496
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kishore Megha¹,Krishnamoorthy G.²,Udgaonkar Jayant B.¹

Affiliation:

1. National Centre for Biological Sciences, Tata Institute of Fundamental Research, Bangalore 560065, India

2. Department of Chemical Sciences, Tata Institute of Fundamental Research, Mumbai 400005, India

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi401337k

Reference65 articles.

1. SH3 domains: complexity in moderation

2. Revealing a Concealed Intermediate that Forms after the Rate-limiting Step of Refolding of the SH3 Domain of PI3 Kinase

3. Four-State Folding of a SH3 Domain: Salt-Induced Modulation of the Stabilities of the Intermediates and Native State

4. Evidence for Initial Non-specific Polypeptide Chain Collapse During the Refolding of the SH3 Domain of PI3 Kinase

5. Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration

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