Journal
JOURNAL OF BIOMOLECULAR NMR
Volume 60, Issue 4, Pages 203-208Publisher
SPRINGER
DOI: 10.1007/s10858-014-9868-5
Keywords
CEST; Conformationally excited protein states; C-13(alpha/beta) chemical shifts; Chemical exchange; Fyn SH3; Protein folding
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Funding
- Canadian Institutes of Health Research (CHIR)
- CIHR
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A pair of triple resonance based CEST pulse schemes are presented for measuring C-13(alpha) and C-13(beta) chemical shifts of sparsely populated and transiently formed conformers that are invisible to traditional NMR experiments. CEST profiles containing dips at resonance positions of C-13(alpha) or C-13(beta) spins of major (ground) and minor (excited) conformers are obtained in a pseudo 3rd dimension that is generated by quantifying modulations of cross peaks in N-15, H-1(N) correlation spectra. An application to the folding reaction of a G48A mutant of the Fyn SH3 domain is presented, illustrating and validating the methodology.
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