title: Biophysical constraints for protein structure prediction.
abstract: 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%.
authors.affiliation: Department of Biochemistry and Molecular Biology, Georgetown University School of Medicine, Washington DC, 20007, USA, ovt@georgetown.edu
authors.forename: Olga
authors.initials: O
authors.lastname: Tcherkasskaya
authors.forename: Eugene A
authors.initials: EA
authors.lastname: Davidson
authors.forename: Vladimir N
authors.initials: VN
authors.lastname: Uversky
mesh_terms: 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
chemical_list: D010455:Peptides; D011506:Proteins; D020543:Proteome