Abstract
Proteins exhibit a variety of internal motions that are, in many cases, necessary for function. Yet, most approaches used to convert NMR data into a three dimensional structure assume a rigid model in translating cross-relaxation data into proton-proton distance constraints. For some types of motion this can lead to substantial errors in the final structure determined. Means of recognizing the presence of significant internal motions and means of minimizing the impact on the structures determined are discussed. Data on a small protein important in fatty acid biosynthesis, acyl carrier protein from spinach, are used to illustrate the procedures.
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References
K. Wüthrich, Meth. Enzymol. 177, 125–131 (1989).
G. A. Borgias and T. L. James, J. Magn. Reson. 79, 493–512 (1988).
G. Lipari and A. Szabo, J. Am. Chem. Soc. 104, 4546–4559 (1982).
D. M. LeMaster, L. E. Kay, A. T. Brünger, and J. H. Prestegard, FEBS Lett. 236, 71–76 (1988).
J. B. Ohlrogge, “The Biochemistry of Plants 9”, P. K. Strumpf, ed., pp. 137-157 (1987).
T. A. Holak, S. K. Kearsley, Y. Kim, and J. H. Prestegard, Biochemistry 27, 6135–6142 (1988).
Y. Kim, J. B. Ohlrogge, and J. H. Prestegard, Biochem. Pharm. 40, 7–13 (1990).
Y. Kim and J. H. Prestegard, J. Am. Chem. Soc. 112, 3707–3709 (1990).
U. C. Singh, P. K. Weiner, D. A. Case, J. Caldwell, and P. A. Kollman, AMBER 3.0 (A program obtained through a licensing agreement with the Regents of the University of California at San Francisco) (1986).
Y. Kim and J. H. Prestegard, Biochemistry 28, 8792–8797 (1989).
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© 1991 Springer Science+Business Media New York
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Prestegard, J.H., Kim, Y. (1991). Structural Interpretation of NMR Data in the Presence of Motion. In: Hoch, J.C., Poulsen, F.M., Redfield, C. (eds) Computational Aspects of the Study of Biological Macromolecules by Nuclear Magnetic Resonance Spectroscopy. NATO ASI Series, vol 225. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9794-7_20
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DOI: https://doi.org/10.1007/978-1-4757-9794-7_20
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