1JXY: CRAMBIN MIXED SEQUENCE FORM AT 220 K. PROTEIN/WATER SUBSTATES

Citation:
Abstract
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.
PDB ID: 1JXYDownload
MMDB ID: 163432
PDB Deposition Date: 2001/9/10
Updated in MMDB: 2018/06
Experimental Method:
x-ray diffraction
Resolution: 0.89  Å
Source Organism:
Similar Structures:
Biological Unit for 1JXY: monomeric; determined by author
Molecular Components in 1JXY
Label Count Molecule
Protein (1 molecule)
1
Crambin
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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