title: The C-terminal domain of the utrophin tandem calponin-homology domain appears to be thermodynamically and kinetically more stable than the full-length protein.
abstract: Domains are in general less stable than the corresponding full-length proteins. Human utrophin tandem calponin-homology (CH) domain seems to be an exception. Reversible, equilibrium denaturant melts indicate that the isolated C-terminal domain (CH2) is thermodynamically more stable than the tandem CH domain. Thermal melts show that CH2 unfolds at a temperature higher than that at which the full-length protein unfolds. Stopped-flow kinetics indicates that CH2 unfolds slower than the full-length protein, indicating its higher kinetic stability. Thus, the utrophin tandem CH domain may be one of the few proteins in which an isolated domain is more stable than the corresponding full-length protein.
authors.affiliation: Department of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado Anschutz Medical Campus , 12850 East Montview Boulevard, C238, Aurora, Colorado 80045, United States .
authors.forename: Swati
authors.initials: S
authors.lastname: Bandi
authors.forename: Surinder M
authors.initials: SM
authors.lastname: Singh
authors.forename: Krishna M G
authors.initials: KM
authors.lastname: Mallela
mesh_terms: D019540:Area Under Curve; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D002850:Chromatography, Gel; D007700:Kinetics; D008840:Microfilament Proteins / Q000737:chemistry*; D013816:Thermodynamics; D049411:Utrophin / Q000737:chemistry*; D000096985:Calponins
chemical_list: D002135:Calcium-Binding Proteins; D008840:Microfilament Proteins; D049411:Utrophin; D000096985:Calponins