title: Thermodynamic insights into proteins from NMR spin relaxation studies.
abstract: NMR spin relaxation measurements of picosecond to nanosecond timescale backbone and sidechain fluctuations of protein molecules, and subsequent entropic interpretation yield interesting, but sometimes counterintuitive, insights into proteins. The stabilities of proteins and protein interactions are achieved through enthalpy-entropy compensation, which is partitioned between the backbone and sidechains depending on the nature of the system.
authors.affiliation: Department of Biochemistry, University of Alberta, Edmonton, Canada. leo.spyracopoulos@ualberta.ca
authors.forename: L
authors.initials: L
authors.lastname: Spyracopoulos
authors.forename: B D
authors.initials: BD
authors.lastname: Sykes
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry; D064026:Calbindins; D002147:Calmodulin / Q000737:chemistry; D030562:Databases, Protein; D019277:Entropy; D051379:Mice; D009219:Myosin-Light-Chain Kinase / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D012260:Ribonucleases / Q000737:chemistry; D064030:S100 Calcium Binding Protein G / Q000737:chemistry; D013816:Thermodynamics
chemical_list: D001426:Bacterial Proteins; D064026:Calbindins; D002147:Calmodulin; C034284:IgG Fc-binding protein, Streptococcus; D011506:Proteins; D064030:S100 Calcium Binding Protein G; C035737:major urinary proteins; C057438:barstar protein, Bacillus amyloliquefaciens; D009219:Myosin-Light-Chain Kinase; D012260:Ribonucleases; C019760:Bacillus amyloliquefaciens ribonuclease