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Determinants of pH sensing folds using backbone residual dipolar coupling and long range NOE restraints

Lookup NU author(s): Professor Steve Homans

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Abstract

We report the determination of the global fold of human ubiquitin using protein backbone NMR residual dipolar coupling and long-range nuclear Overhauser effect (NOE) data as conformational restraints. Specifically, by use of a maximum of three backbone residual dipolar couplings per residue (Ni-HN i, Ni-Ci–1, HN i - Ci–1) in two tensor frames and only backbone HN-HN NOEs, a global fold of ubiquitin can be derived with a backbone root-mean-square deviation of 1.4 Å with respect to the crystal structure. This degree of accuracy is more than adequate for use in databases of structural motifs, and suggests a general approach for the determination of protein global folds using conformational restraints derived only from backbone atoms.

Publication metadata

Author(s): Giesen AW, Homans SW, Brown JM

Publication type: Article

Publication status: Published

Journal: Journal of Biomolecular NMR

Year: 2003

Volume: 25

Issue: 1

Pages: 63-71

ISSN (print): 0925-2738

ISSN (electronic): 1573-5001

Publisher: Springer Netherlands

URL: http://dx.doi.org/10.1023/A:1021954812977

DOI: 10.1023/A:1021954812977

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