Global folds of proteins with low densities of NOEs using residual dipolar couplings: Application to the 370-residue maltodextrin-binding protein

Journal of Molecular Biology

Volumn 300, Issue 1, 2000, Pages 197-212

  Mueller, Geoffrey A ^a,b   Choy, W Y ^a,b   Yang, Daiwen ^a   Forman Kay, Julie D ^b   Venters, Ronald A ^c   Kay, Lewis E ^a  

^a UNIVERSITY OF TORONTO   (Canada)

^b HOSPITAL FOR SICK CHILDREN   (Canada)

^c DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

Dipolar couplings; Labeling; Maltodextrin binding protein; Protein domains; Protein structure

Indexed keywords

BETA CYCLODEXTRIN; BINDING PROTEIN; CARBON 13; DEUTERIUM; ISOLEUCINE; LEUCINE; MALTODEXTRIN; MALTOSE BINDING PROTEIN; NITROGEN 15; VALINE;

ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; DIPOLE; HYDROGEN BOND; MOLECULAR WEIGHT; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING;

EID: 0034733394     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3842     Document Type: Article

References (54)

1. Multidimensional nuclear magnetic resonance methods for protein studies
2. Solution structure of cyanovirin-N, a potent HIV-inactivating protein
3. Crystallography and NMR system: A new software system for macromolecular structure determination
4. Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration
5. A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information
6. Direct structure refinement against residual dipolar couplings in the presence of rhombicity of unknown magnitude
7. Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses
8. Impact of residual dipolar couplings on the accuracy of NMR structures determined from a minimal number of NOE restraints
9. Protein backbone angle restraints from searching a database for chemical shift and sequence homolgy
10. NMRPipe: A multidimensional spectral processing system based on UNIX pipes
11. Protein structure determination using molecular fragment replacement and NMR dipolar couplings
12. NMR of perdeuterated large proteins
13. Domain orientation and dynamics in multidomain proteins from residual dipolar couplings
14. Global folds of highly deuterated, methyl protonated proteins by multidimensional NMR
15. 15N multidimensional NMR to study the structure and dynamics of proteins
16. Solution NMR studies of a 42 kDa E. coli maltose binding protein/β cyclodextrin complex: Chemical shift assignments and analysis
17. Band-selective radio-frequency pulses
18. 2H-labeled proteins
19. 15N-enriched proteins. Application to HIV-1 Nef.
20. Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions
21. Three-dimensional structure of β-galactosidase from E. coli
22. NMRView: A computer program for the visualization and analysis of NMR data
23. Structure of a unique binuclear manganese cluster in arginase
24. MOLMOL: A program for display and analysis of macromolecular structures
25. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
26. 13C(α) chemical shifts in protein structure refinement
27. NOE data demonstrating a compact unfolded state for an SH3 domain under nondenaturing conditions
28. 13C-edited NOESY experiment
29. SCOP: A structural classification of proteins database for the investigation of sequences and structures
30. Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2
31. 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
32. 13C-labeled proteins
33. Selective methyl group protonation of perdeuterated proteins
34. A constant-time 2D overbodenhausen experiment for inverse correlation of isotopically enriched species
35. Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis
36. Refined 1.8-Å structure reveals the mode of binding of β-cyclodextrin to the maltodextrin binding protein
37. Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: Differences in solution and crystal forms of maltodextrin binding protein loaded with β-cyclodextrin
38. The 2.3-Å resolution structure of the maltose or malto-dextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
39. Torsion-angle molecular dynamics as a new efficient tool for NMR structure calculation
40. Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-Å resolution
41. Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
42. 13C couplings in the structure determination of magnetically oriented macromolecules in solution
43. Nuclear magnetic dipole interactions in field-oriented proteins: Information for structure determination in solution
44. Structure and energetics of a non-proline cis-peptidyl linkage in a pro-line-202 → alanine carbonic anhydrase II variant
45. 1H assignments of human carbonic arthydrase II
46. 1HN NOEs to determine protein global folds in perdeuterated proteins
47. 13C decoupling
48. NMR spectroscopy of large molecules and multimolecular assemblies in solution
49. 13C chemical-shift data
50. 2H-labeled proteins
51. Model of maltose-binding protein/chemoreceptor complex supports intrasubunit signaling mechanism
52. 13C labeled proteins with high resolution
53. 2H-labeled proteins