NDLI: Energy landscape along an enzymatic reaction trajectory: hinges orcracks?

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Energy landscape along an enzymatic reaction trajectory: hinges orcracks?

Content Provider	PubMed Central
Author	Whitford, Paul Charles Onuchic, José Nelson Wolynes, Peter Guy
Copyright Year	2008
Abstract	Are the most dynamically flexible regions around the equilibrium structureof an enzyme the same regions involved in the transition state forrate limiting processes involved in the enzymatic reaction? Kern and-coworkers(Wolf-Watzet al., 2004; Henzler-Wildman et al., 2007a, 2007b)have shown that insights about functionally relevant motions that determinethe overall enzyme turnover rate can be obtained by investigating conformationaldynamics around the equilibrium basin of the enzyme adenylate kinase. An allostericchange in protein structure turns out to be the controlling process. In thiscommentary we compare results of this study with earlier predictions of theroute by which the enzyme undergoes its conformational change. These predictionsare based on the idea that the energy surface for the protein is determinedby the end structures of the conformational change. A key issue is whetherthe protein moves by specific hinges or whether it “cracks”and accesses partially unfolded states during its structural change.
Related Links	http://dx.doi.org/10.2976/1.2894846
Ending Page	64
Page Count	4
Starting Page	61
File Format	PDF
ISSN	19552068
e-ISSN	1955205X
Journal	HFSP Journal
Issue Number	2
Volume Number	2
Language	English
Publisher	HFSP Publishing
Publisher Date	2008-04-01
Access Restriction	Open
Rights Holder	HFSP Publishing
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience Biochemistry, Genetics and Molecular Biology

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