Abstract
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, an approach which minimizes the degree of water saturation is employed, enabling the extraction of accurate rate constants.
MeSH Terms
Chemical Phenomena
Chemistry, Physical
Drosophila Proteins
Insect Hormones/chemistry
Magnetic Resonance Spectroscopy/methods
Nitrogen Isotopes
Protein Structure, Tertiary
Chemicals
Drosophila Proteins
Insect Hormones
Nitrogen Isotopes
drk protein, Drosophila
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Farrow N A
Protein Engineering Network Centres of Excellence, University of Toronto, ON, Canada.
Zhang O
Forman-Kay J D
Kay L E
References (6)
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