Please use this identifier to cite or link to this item: https://doi.org/10.1023/B:JNMR.0000013826.82936.0e
Title: Measurement of dipolar cross-correlation in methylene groups in uniformly 13C-, 15N-labeled proteins
Authors: Zheng, Y. 
Yang, D. 
Keywords: Cross-correlated relaxation
Fatty acid binding protein
Protein side chain dynamics
Issue Date: Feb-2004
Citation: Zheng, Y., Yang, D. (2004-02). Measurement of dipolar cross-correlation in methylene groups in uniformly 13C-, 15N-labeled proteins. Journal of Biomolecular NMR 28 (2) : 103-116. ScholarBank@NUS Repository. https://doi.org/10.1023/B:JNMR.0000013826.82936.0e
Abstract: A CC(CO)NH TOCSY-based 3D pulse scheme is presented for measuring 1H-13C dipole-dipole cross-correlated relaxation at CH2 positions in uniformly 13C-, 15N-labeled proteins. Simulations based on magnetization evolution under relaxation and scalar coupling interactions show that cross-correlation rates between 1H-13C dipoles in CH2 groups can be simply obtained from the intensities of 13C triplets. The normalized cross-correlation relaxation rates are related to cross-correlation order parameters for macromolecules undergoing isotropic motion, which reflect the degrees of spatial restriction of CH2 groups. The study on human intestinal fatty acid binding protein (131 residues) in the presence of oleic acid demonstrates that side chain dynamics at most CH2 positions can be characterized for proteins less than 15 kDa in size, with the proposed TOCSY-based approach.
Source Title: Journal of Biomolecular NMR
URI: http://scholarbank.nus.edu.sg/handle/10635/101067
ISSN: 09252738
DOI: 10.1023/B:JNMR.0000013826.82936.0e
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