A view of dynamics changes in the molten globulenative folding step by quasielastic neutron scattering

Journal of Molecular Biology

Volumn 301, Issue 2, 2000, Pages 525-536

  Bu, Zimei ^a   Neumann, Dan A ^a   Lee, Seung Hun ^a   Brown, Craig M ^a   Engelman, Donald M ^b   Han, Charles C ^a  

^a NATIONAL INSTITUTE OF STANDARDS AND TECHNOLOGY   (United States)

^b YALE UNIVERSITY   (United States)

Author keywords

Molten globule; Protein dynamics; Protein folding dynamics; Quasielastic neutron scattering; Lactalbumin

Indexed keywords

ALPHA LACTALBUMIN;

ARTICLE; CATTLE; MOLECULAR DYNAMICS; NEUTRON SCATTERING; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; THERMODYNAMICS; VIBRATION;

BOS TAURUS; BOVINAE;

EID: 0034636990     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3978     Document Type: Article

References (56)

1. On the temperature dependence of cooperative relaxation properties in glass-forming liquids
2. Structure and dynamics of the acid-denatured molten globule state of alphalactalbumin: A two-dimensional NMR study
3. A kinetic model for the internal motions of proteins: Diffusion between multiple harmonic wells
4. Side-chain accessibility and dynamics in the molten globule state of alpha-lactalbumin: A 19F-NMR study
5. Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig alpha-lactalbumin
6. Neutron investigation of reorientations in organic molecular compounds
7. Dynamics of hydration water in protein
8. Entropy in protein folding and in protein-protein interactions
9. Spin glasses and the statistical mechanics of protein folding
10. Intermediates and barrier crossing in a random energy model (with applications to protein folding)
11. Neutron time-of-flight spectroscopy
12. Hydration of denatured and molten globule proteins
13. Dominant forces in protein folding
14. Protein folding. Solid evidence for molten globules
15. The fundamentals of protein folding: Bringing together theory and experiment
16. Side-chain conformational entropy in protein folding
17. Growing spatial correlations of particle displacements in a simulated liquid on cooling toward the glass transition
18. Microscale and macroscale diffusion of water in colloidal gels. A pulsed field gradient and NMR imaging investigation
19. The energy landscapes and motions of proteins
20. Compactness of the kinetic molten globule of bovine alpha-lactalbumin: A dynamic light scattering study
21. Energetics of solvent and ligand-induced conformational changes in alpha-lactalbumin
22. Kinetics and thermodynamics of folding of a de novo designed four-helix bundle protein
23. Energetics of structural domains in alpha-lactalbumin
24. Collective motions in proteins: A covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations
25. Dynamics of proteins: Elements and function
26. Configurational entropy of native proteins
27. Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering
28. Dynamical and structural modifications of staphylococcal nuclease on C-terminal truncation
29. Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A
30. The molten globule state of alphalactalbumin
31. Protein folding: The endgame
32. The introduction of strain and its effects on the structure and stability of T4 lysozyme
33. Evolutionarily conserved pathways of energetic connectivity in protein families
34. Energetics of protein structure
35. Studies on protein stability with T4 lysozyme
36. A protein dissection study of a molten globule
37. Does the molten globule have a native-like tertiary fold?
38. Crystal structures of guinea-pig, goat and bovine alpha-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase
39. Molten globule and protein folding
40. Dynamics of different functional parts of bacteriorhodopsin: H-2H labeling and neutron scattering
41. Picosecond dynamical changes on denaturation of yeast phosphoglycerate kinase revealed by quasielastic neutron scattering
42. Alpha-lactalbumin forms a compact molten globule in the absence of disulfide bonds
43. Areas, Volumes, packing, and protein structure
44. An analysis of packing in the protein folding problem
45. A residue-specific NMR view of the non-cooperative unfolding of a molten globule
46. The denatured state (the other half of the folding equation) and its role in protein stability
47. Protein dynamics: Comparison of simulations with inelastic neutron scattering experiments
48. Neutron incoherent scattering law for diffusion in a potential of spherical symmetry: General formalism and application to diffusion inside a sphere
49. The native-like tertiary fold in molten globule alpha-lactalbumin appears to be controlled by a continuous phase transition
50. Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
51. A specific hydrophobic core in the alpha-lactalbumin molten globule
52. Bipartite structure of the alpha-lactalbumin molten globule
53. How soft is a protein? A protein dynamics force constant measured by neutron scattering