Predicting the energetics of conformational fluctuations in proteins from sequence: a strategy for profiling the proteome.
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.
Gu
Jenny
J
Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, 77555-1068, USA.
Hilser
Vincent J
VJ
D000465:Algorithms; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D007700:Kinetics; D008958:Models, Molecular; D011237:Predictive Value of Tests; D011487:Protein Conformation; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D020543:Proteome / Q000737:chemistry*; D015203:Reproducibility of Results; D016415:Sequence Alignment
D000596:Amino Acids; D011506:Proteins; D020543:Proteome