Characterizing domain interfaces by NMR.
The combination of chemical shift, residual dipolar coupling, and backbone relaxation data can be used to characterize the nature of a domain interface in a multidomain protein. Comparison of the parameters obtained from isolated domains and domain pairs provides insight into the composition of the interface as well as into interdomain dynamics. The interface between the 13th and 14th F3 module from fibronectin is used as an example.
Department of Biochemistry, University of Oxford, UK.
Luke M
LM
Rooney
Sachchidanand
Jörn M
JM
Werner
D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*
D011506:Proteins