Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain.
A novel off-resonance rotating-frame 15N NMR spin relaxation experiment is used to characterize conformational fluctuations with correlation times between 32 and 175 microseconds in the third fibronectin type III domain of human tenascin-C. Conformational fluctuations of contiguous regions of the beta-sandwich structure of the type III domain may represent collective motions, such as transient twisting or breathing of the beta-sheets. Flexibility of the loop containing the Arg-Gly-Asp (RGD) tripeptide may affect the accessibility of this motif in protein-protein interactions.
Akke
M
M
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA.
Liu
J
J
Cavanagh
J
J
Erickson
H P
HP
Palmer
A G
AG
D004058:Diffusion; D019281:Dimerization; D005353:Fibronectins / Q000737:chemistry*; D006801:Humans; D006860:Hydrogen Bonding; D009038:Motion; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D019063:Tenascin / Q000737:chemistry*
D005353:Fibronectins; D019063:Tenascin