Biophysical constraints for protein structure prediction.
Though highly desirable, neither a single experimental technique nor a computational approach can be sufficient enough to rationalize a protein structure. The incorporation of biophysical constraints, which can be rationalized based on conventional biophysical measurements, might lead to considerable improvement of the simulation procedures. In this regard, our analysis of 180 proteins in different conformational states allows prediction of the overall protein dimension based on the chain length, i.e., the protein molecular weight, with an accuracy of 10%.
Tcherkasskaya
Olga
O
Department of Biochemistry and Molecular Biology, Georgetown University School of Medicine, Washington DC, 20007, USA, ovt@georgetown.edu
Davidson
Eugene A
EA
Uversky
Vladimir N
VN
D000465:Algorithms; D000818:Animals; D001703:Biophysics / Q000379:methods; D019992:Databases as Topic; D006801:Humans; D015233:Models, Statistical; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000032:analysis / Q000737:chemistry*; D020543:Proteome; D015203:Reproducibility of Results; D012984:Software; D013816:Thermodynamics
D010455:Peptides; D011506:Proteins; D020543:Proteome