The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins

Annual Review of Biophysics and Biomolecular Structure

Volumn 27, Issue , 1998, Pages 357-406

  Gardner, Kevin H ^a   Kay, Lewis E ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

Amino acid specific isotopic labeling; Protein deuteration; Sidechain dynamics; Structure determination; Triple resonance NMR

Indexed keywords

CARBON NUCLEAR MAGNETIC RESONANCE; DYNAMICS; HUMAN; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; PROTEIN TRANSPORT; PROTON NUCLEAR MAGNETIC RESONANCE; REVIEW; STRUCTURE ANALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; ESCHERICHIA COLI; METABOLISM; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION; SENSITIVITY AND SPECIFICITY;

CARBON; DEUTERIUM; NITROGEN; PROTEIN; RECOMBINANT PROTEIN;

CARBON ISOTOPES; DEUTERIUM; ESCHERICHIA COLI; MODELS, MOLECULAR; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEINS; RECOMBINANT PROTEINS; SENSITIVITY AND SPECIFICITY;

EID: 0031595590     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.27.1.357     Document Type: Review

References (14)

1. 2 relaxation rates of the protons in the partially deuterated and fully protonated sugar residues in a large oligo-DNA ('NMR-window') gives complementary structural information. Nucl. Acids Res. 22:1404-12
2. Allerhand A, Doddrell D, Glushko V, Cochran DW, Wenkert E, et al. 1971. Conformational and segmental motion of native and denatured ribonuclease A in solution. Application of natural abundance carbon-13 partially relaxed Fourier transform nuclear magnetic resonance. J. Am. Chem. Soc. 93:544-6
3. Anglister J. 1990. Use of deuterium labelling in NMR studies of antibody combining site structure. Q. Rev. Biophys. 23:175-203
4. 1H NMR assignments and secondary structure in solution of Escherichia coli trp repressor. Biochemistry 29:6332-41
5. 1H NMR assignment of larger proteins. Die Makromol. Chem., Macromol. Symp. 34:33-46
6. Aszódi A, Gradwell MJ, Taylor WR. 1995. Global fold determination from a small number of distance restraints. J. Mol. Biol. 251:308-26
7. Bastiaan EW, Maclean C, Van Zijl PCM, Bothner-By AA. 1987. High-resolution NMR of liquids and gases: effects of magnetic-field-induced molecular align-ment. Annu. Rep. NMR. Spec. 19:35-77
8. 15N labeling and random fractional deuteration of ribonucleotides. Nucl. Acids Res. 24:4836-37
9. Bax A. 1994. Multidimensional nuclear magnetic resonance methods for protein studies. Curr. Opin. Struct. Biol. 4:738-44
10. Bax A, De Jong DE, Mehlkopf AF, Smidt J. 1980. Separation of the different orders of NMR multiple-quantum transitions by the use of pulsed field gradients. Chem. Phys. Lett. 69:567-70
11. 1H spectra using gradient pulses for coherence-transfer-pathway selection. J. Magn. Reson. 98:660-64
12. Brodin P, Drakenberg T, Thulin E, Forsén S, Grundström T. 1989. Selective proton labelling of amino acids in deuterated bovine calbindin D9k. A way to simplify NMR spectra. Prot. Eng. 2:353-58
13. 13C nuclear magnetic resonance. II. A specific labeling approach to the study of histidine residues in proteins. J. Am. Chem. Soc. 95:1316-23
14. Cavanagh J, Rance M. 1988. Sensitivity improvement in isotropic mixing (TOCSY) experiments. J. Magn. Reson. 88:72-85