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Comment

. 2013 Apr 30;110(18):7114-5.

doi: 10.1073/pnas.1305236110. Epub 2013 Apr 22.

Disorder guides protein function

Paul C Whitford¹

Affiliations

PMID: 23610426
PMCID: PMC3645555
DOI: 10.1073/pnas.1305236110

Comment

Disorder guides protein function

Paul C Whitford. Proc Natl Acad Sci U S A. 2013.

. 2013 Apr 30;110(18):7114-5.

doi: 10.1073/pnas.1305236110. Epub 2013 Apr 22.

Author

Paul C Whitford¹

Affiliation

¹ Department of Physics, Northeastern University, Boston, MA 02115, USA. p.whitford@neu.edu

PMID: 23610426
PMCID: PMC3645555
DOI: 10.1073/pnas.1305236110

No abstract available

PubMed Disclaimer

Conflict of interest statement

The author declares no conflict of interest.

Figures

Fig. 1. — Fig. 1.
Partial unfolding during function, known as cracking (2), was predicted to be a general property that allows proteins to reduce free-energy barriers and accelerate functional kinetics. In EGFR kinase, crystal structures of the active (Left) and inactive (Right) forms might suggest that interconversion can be fully described by simple displacements/rotations. Through the use of many-microsecond molecular dynamics simulations, Shan et al. (6) has directly observed specific residues (circled) partially unfolding and refolding during this transition.

See this image and copyright information in PMC

Comment on

Transitions to catalytically inactive conformations in EGFR kinase.
Shan Y, Arkhipov A, Kim ET, Pan AC, Shaw DE. Shan Y, et al. Proc Natl Acad Sci U S A. 2013 Apr 30;110(18):7270-5. doi: 10.1073/pnas.1220843110. Epub 2013 Apr 1. Proc Natl Acad Sci U S A. 2013. PMID: 23576739 Free PMC article.

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