Journal
STRUCTURE
Volume 16, Issue 11, Pages 1627-1637Publisher
CELL PRESS
DOI: 10.1016/j.str.2008.08.016
Keywords
-
Funding
- NIGMS NIH HHS [R01 GM063747, GM13747, R01 GM063747-07] Funding Source: Medline
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available