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2004 | 53 | 3-4 | 263-270
Article title

Spektroskopia magnetycznego rezonansu jądrowego w wyznaczaniu budowy białek

Title variants
Nuclear magnetic resonance spectroscopy in the determination of protein structures
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Summary Nuclear magnetic resonance spectroscopy (NMR) is a method well suited to play an important part in proteomics programs. It provides structural information at the atomic resolution. Isotopes of biologically important elements, 1H, 13C, 15N, and 31P, display narrow resonance lines while the most abundant nitrogen (14N) and carbon (12C) isotopes are uselessness in the NMR studies of macromolecules. Internuclear interactions, modulated by even small structural and conformational changes, influence line shape and intensity of signals in NMR spectra. Last but not least, NMR provides high resolution structures in solution allowing to study those proteins that fail to crystallize or to compare differences between their crystal and solution structures. The pros and cons of NMR spectroscopy as a tool for the protein structure determination are discussed. Recently, the advance in the NMR equipment, spectral techniques and isotope labelling resulted in an enormous growth of the number of NMR-determined protein structures. Modern NMR-based procedure of structure determination comprises three stages: assignment of as many signals as possible in the spectra of NMR-active isotopes, identification of structural constraints, and calculation of a family of three-dimensional structures fulfilling experimental constraints. Approaches used at the first two stages depend on the size of the protein studied whereas the approach applied at the third stage depends on the type and number of identified constraints.
Physical description
  • Instytut Biochemii i Biofizyki PAN, Pawińskiego 5A, 02-106 Warszawa, Polska
  • BAX A., GRZESIEK S., 1993. Methodological Advances in Protein NMR. Acc. Chem. Res. 26, 131-138.
  • BECKER E. D., FISK C., KHETRAPAL C. L., 1996. The Development of NMR. [W:] Encyclopedia of Nuclear Magnetic Resonance. GRANT D. M., HARRIS R. K. (red.). John Wiley, Chichester 1, 1-158.
  • CLORE G. C., GRONENBORN A. M., 1998. Determining Structures of Large Proteins and Protein Complexes byNMR. [W:] BiologicalMagnetic Resonance. KRISHNA N. R., BERLINER L. J. (red.). Kluwer Academic/ Plenum Publishers, New York 16, 3-26.
  • DYSON H. J., WRIGHT P. E., 1994. Protein Structure Calculation Using NMR Restraints. [W:] Two-Dimensional NMR Spectroscopy. Application for Chemists and Biochemists. Second Edition. CROASMUN W. R., CARLSON R. M. K. (red.). VCH Publishers Inc., New York.
  • EJCHART A., 1999. Scalar Couplings in Structure Determination of Proteins. Bull. Pol. Ac.: Chem. 47, 1-19.
  • EJCHART A., GRYFF-KELLER A., 2000. Wpływ częściowego uporządkowania orientacji cząsteczek na ich widma NMR dużej zdolności rozdzielczej. Wiad. Chem. 54. 949-969.
  • FRIEBOLIN H., 1999. Basic Oneand Two-Dimensional NMR Spectroscopy. Wyd. 3 poprawione. VCH Publishers Inc., Weinheim.
  • KAY L. E., 2001. Nuclear Magnetic Resonance Methods for High Molecular Weight Proteins: A Study Involving a Complex of Maltose Binding Protein and β-Cyclodextrin. [W:] Methods in Enzymology. JAMES T. L., DÖTSCH V., SCHMITZ U. (red.). Academic Press, San Diego 339, 174-203.
  • LIAN L.-Y., MIDDLETON D. A., 2001. Labelling approaches for protein structured studies by solutionstate and solid-state NMR. Prog. Nucl. Magn. Reson. Spectrosc. 39, 171-190.
  • NEUHAUS D.,WILLIAMSON M. P., 1989. The Nuclear Overhauser Effect in Structural and Conformational Analysis. VCH Publishers Inc., New York.
  • VAN DE VEN F. J. M., 1995. Multidimensional NMR in Liquids. VCH Publishers Inc., New York.
  • WÜTHRICH K., 1986. NMR of Proteins and Nucleic Acids. Wiley, New York.
  • ZHUKOV I., 2001. Solution structure and backbone dynamics of CMTI-I (Met8>Leu) and bovine apo-S100A1(αα) proteins as studied byNMR spectroscopy. Praca doktorska, IBB PAN, Warszawa.
  • ZHUKOV I., EJCHART A., 2003.NMRspectroscopy in structural proteomics. NMR-based protein structure determination. Polimery 48, 28-34.
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