A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium |
| |
| Authors: | Neil A Farrow Ouwen Zhang Julie D Forman-Kay Lewis E Kay |
| |
| Institution: | (1) Protein Engineering Network Centres of Excellence, University of Toronto, M5S 1A8 Toronto, ON, Canada;(2) Department of Molecular and Medical Genetics, University of Toronto, M5S 1A8 Toronto, ON, Canada;(3) Department of Biochemistry, University of Toronto, M5S 1A8 Toronto, ON, Canada;(4) Department of Chemistry, University of Toronto, M5S 1A8 Toronto, ON, Canada;(5) Division of Biochemistry Research, Hospital for Sick Children, 555 University Avenue, M5G 1X8 Toronto, ON, Canada |
| |
| Abstract: | Summary A heteronuclear correlation experiment is described which permits simultaneous characterization of both 15N longitudinal decay rates and slow conformational exchange rates. Data pertaining to the exchange between folded and unfolded forms of an SH3 domain is used to illustrate the technique. Because the unfolded form of the molecule, on average, shows significantly higher NH exchange rates than the folded form, and approach which minimizes the degree of water saturation is employed, enabling the extraction of accurate rate constants. |
| |
| Keywords: | Protein dynamics Chemical exchange Protein folding |
| 本文献已被 SpringerLink 等数据库收录！ |
|
