title: Exploring regions of conformational space occupied by two-domain proteins.
abstract: The presence of heterogeneity in the interdomain arrangement of several biomolecules is required for their function. Here we present a method to obtain crucial clues to distinguish between different kinds of protein conformational distributions based on experimental NMR data. The method explores subregions of the conformational space and provides both upper and lower bounds of probability for the system to be in each subregion.
authors.affiliation: Center for Magnetic Resonance, University of Florence , Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.
authors.forename: Witold
authors.initials: W
authors.lastname: Andrałojć
authors.forename: Claudio
authors.initials: C
authors.lastname: Luchinat
authors.forename: Giacomo
authors.initials: G
authors.lastname: Parigi
authors.forename: Enrico
authors.initials: E
authors.lastname: Ravera
mesh_terms: D002147:Calmodulin / Q000737:chemistry; D003198:Computer Simulation; D064550:Death-Associated Protein Kinases / Q000737:chemistry; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*
chemical_list: D002147:Calmodulin; D010455:Peptides; D011506:Proteins; D064550:Death-Associated Protein Kinases