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Protein dynamics studied by rotating frame15N spin relaxation times

✍ Scribed by T. Szyperski; P. Luginbühl; G. Otting; P. Güntert; K. Wüthrich

Publisher
Springer Netherlands
Year
1993
Tongue
English
Weight
877 KB
Volume
3
Category
Article
ISSN
0925-2738

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✦ Synopsis

Conformational rate processes in aqueous solutions of uniformly ~SN-labeled pancreatic trypsin inhibitor (BPTI) at 36 ~ were investigated by measuring the rotating frame relaxation times of the backbone 15N spins as a function of the spin-lock power. Two different intramolecular exchange processes were identified. A first local rate process involved the residues Cys 38 and Arg 39, had a correlation time of about 1.3 ms, and was related to isomerization of the chirality of the disulfide bond Cys14-Cys 3s. A second, faster motional mode was superimposed on the disulfide bond isomerization and was tentatively attributed to local segmental motions in the polypeptide sequence -Cys 14 -Ala 15 -Lys 16 -. The correlation time for the overall rotational tumbling of the protein was found to be 2 ns, using the assumption that relaxation is dominated by dipolar coupling and chemical shift anistropy modulated by isotropic molecular reorientation.

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