1jxx
From Proteopedia
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| , resolution 0.89Å | |||||||
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CRAMBIN MIXED SEQUENCE FORM AT 200 K. PROTEIN/WATER SUBSTATES
Overview
Diverse biochemical and biophysical experiments indicate that all proteins, regardless of size or origin, undergo a dynamic transition near 200 K. The cause of this shift in dynamic behavior, termed a "glass transition," and its relation to protein function are important open questions. One explanation postulated for the transition is solidification of correlated motions in proteins below the transition. We verified this conjecture by showing that crambin's radius of gyration (Rg) remains constant below approximately 180 K. We show that both atom position and dynamics of protein and solvent are physically coupled, leading to a novel cooperative state. This glassy state is identified by negative slopes of the Debye-Waller (B) factor vs. temperature. It is composed of multisubstate side chains and solvent. Based on generalization of Adam-Gibbs' notion of a cooperatively rearranging region and decrease of the total entropy with temperature, we calculate the slope of the Debye-Waller factor. The results are in accord with experiment.
About this Structure
1JXX is a Single protein structure of sequence from Crambe hispanica subsp. abyssinica. Full crystallographic information is available from OCA.
Reference
On the nature of a glassy state of matter in a hydrated protein: Relation to protein function., Teeter MM, Yamano A, Stec B, Mohanty U, Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11242-7. PMID:11572978
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