Abstract
A heteropolar 2D NMR technique for measurement of {sub 13}C T{sub 1} values in proteins previously reported has been applied to the determination of spin-lattice relaxation times for the {gamma}-carbons of basic pancreatic trypsin inhibitor (BPTI). The technique is described in some detail as applied to BPTI. The lack of dramatic variations noted for T{sub 1} values is taken as assurance that measurements of nuclear Overhauser effects for determination of protein structures in solution are not significantly biased by internal motions, at least as far as the backbone of the protein is concerned. 6 refs., 4 figs.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
