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Structure. 2008 Nov 12;16(11):1627-37. doi: 10.1016/j.str.2008.08.016.

Predicting the energetics of conformational fluctuations in proteins from sequence: a strategy for profiling the proteome.

Author information

1
Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, 77555-1068, USA.

Abstract

The abundance of dynamic and disordered regions in proteins suggests that structural determinants alone may not be sufficient to describe function. Instead, descriptors that account for the dynamic features of the energy landscape populated by the protein ensemble may be required. Here, we show that the thermodynamics of the dynamical complexity that imparts biological function can be largely reconstructed using sequence information alone, allowing thermodynamic characterization of entire proteomes without the need for structural analysis. We show that this tool can be used to analyze conserved energetic signatures within classes of proteins, as well as to compare the thermodynamic character of different proteomes.

PMID:
19000815
PMCID:
PMC2674280
DOI:
10.1016/j.str.2008.08.016
[Indexed for MEDLINE]
Free PMC Article

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