Conformational dynamics of cytochalasin B in solution as detected by 13C and 1H NMR relaxation rates.
13C and 1H NMR spin-lattice relaxation rates have been measured for cytochalasin B in [2H]6DMSO. Motional features have been interpreted in terms of nearly isotropic reorientation of the whole molecule with few additional internal motions. The 'isotropic' reorientational correlation time was evaluated at 0.21 ns at room temperature. By using selective and double-selective excitation techniques, relevant cross-relaxation terms have been obtained wherefrom proton-proton distances have been calculated. A Dreiding model of the 'preferred' conformation in solution has been built, yielding evidence of a strong similarity between solution and solid state structures of cytochalasin B.
Gaggelli
E
E
Department of Chemistry, University of Siena, Italy.
Maccotta
A
A
Scopa
A
A
Valensin
G
G
D002247:Carbon Isotopes; D003571:Cytochalasin B / Q000378:metabolism*; D006859:Hydrogen; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D011487:Protein Conformation
D002247:Carbon Isotopes; D003571:Cytochalasin B; D006859:Hydrogen