Structural highlights
Function
[CRAM_CRAAB] The function of this hydrophobic plant seed protein is not known.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Teeter MM, Yamano A, Stec B, Mohanty U. On the nature of a glassy state of matter in a hydrated protein: Relation to protein function. Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11242-7. PMID:11572978 doi:10.1073/pnas.201404398
