Native-like secondary structure of molten globules

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1594, Issue 1, 2002, Pages 168-177

  Vassilenko, Konstantin S ^a   Uversky, Vladimir N ^b,c  

^a INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

^b INSTITUTE FOR BIOLOGICAL INSTRUMENTATION   (Russian Federation)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Circular dichroism; Molten globule; Secondary structure

Indexed keywords

GLOBULAR PROTEIN;

ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; MATHEMATICAL ANALYSIS; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; QUANTITATIVE ANALYSIS; X RAY;

CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; GLOBULINS; HYDROGEN-ION CONCENTRATION; PROTEIN STRUCTURE, SECONDARY; SPECTROPHOTOMETRY, ULTRAVIOLET;

EID: 0037203848     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(01)00303-X     Document Type: Article

References (53)

1. Molten globule and protein folding
2. α-lactalbumin: Compact state with fluctuating tertiary structure?
3. Quasielastic light scattering of human α-lactalbumin: Comparison of molecular dimensions in native and 'molten globule' states
4. Use of fast protein size-exclusion chromatography to study the unfolding of proteins which denature through the molten globule
5. The molten globule state as a clue for understanding the folding and cooperativity of globular protein structure
6. Computed circular dichroism spectra for the evaluation of protein conformation
7. Determination of protein secondary structure
8. Theoretical determination of the CD of proteins containing closely packed antiparallel β-sheets
9. The effect of conformation on the CD of interacting helices: A theoretical study of tropomyosin
10. Aromatic and cystine side-chain circular dichroism in proteins
11. Determination of the secondary structure of proteins from circular dichroism spectra IV. Contribution of aromatic amino acid residues into circular dichroism spectra of proteins in the peptide region (Moscow)
12. Determination of the protein secondary structure from their CD spectra: V. The secondary structure of proteins in a 'molten globule' state (Moscow)
13. Thermodynamic study of the apomyoglobin structure
14. A rapid micromethod for the determination of nitrogen and phosphate in biological material
15. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
16. Automatic identification of secondary structure in globular proteins
17. Estimation of globular protein secondary structure from circular dichroism
18. Two-stage equilibrium unfolding of carbonic anhydrase B by strong denaturants (Moscow)
19. Retinol-binding protein is in the molten globule state at low pH
20. Further evidence on the equilibrium 'pre-molten globule state': Four-state GdmCl-induced unfolding of carbonic anhydrase B at low temperature
21. Three-stage equilibrium unfolding of small globular proteins by strong denaturants: I Carbonic anhydrase B (Moscow)
22. Sensitivity of circular dichroism to protein tertiary structure class
23. Informational content in the circular dichroism of proteins
24. Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins
25. The Protein Data Bank: A computer-based archival file for macromolecular structures
26. Structure determination of the biliverdin apomyoglobin complex: Crystal structure analysis of two crystal forms at 1.4 and 1.5 Å resolution
27. Is apomyoglobin a molten globule? Structural characterization by NMR
28. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding
29. Secondary structures comparison of aquaporin-1 and bacteriorhodopsin: A Fourier transform infrared spectroscopy study of two-dimensional membrane crystals
30. Papaya glutamine cyclase, a plant enzyme highly resistant to proteolysis, adopts an all-beta conformation
31. Secondary structure of homologous proteins, α-fetoprotein and serum albumin, from their circular dichroism and infrared spectra
32. Some problems of CD analyses of protein conformation
33. Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig α-lactalbumin
34. Structural characterization of a partly folded apomyoglobin intermediate
35. Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR
36. Structure and stability of the molten globule state of guinea-pig α-lactalbumin: A hydrogen exchange study
37. The folding of hen lysozyme involves partially structured intermediates and multiple pathways
38. Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy
39. Kinetics of folding of the all-β sheet protein interleukin-1 β
40. A native tertiary interaction stabilizes the A state of cytochrome c
41. Structural basis of the stability of a lysozyme molten globule
42. Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding
43. Packing interactions in the apomyglobin folding intermediate
44. How molten is the molten globule?
45. Compact state of a protein molecule with pronounced small-scale mobility: Bovine α-lactalbumin
46. Acid form of carbonic anhydrase: 'molten globule' with a secondary structure
47. The molten globule state
48. Detection and characterization of the intermediate on the folding pathway of human α-lactalbumin
49. Conformational states of β-lactamase: Molten globule states at acidic and alkaline pH with high salt
50. Folding of ribonuclease A from a partially disordered conformation. Kinetic study under folding conditions
51. Acid denaturation of bovine carbonic anhydrase B
52. Acid-induced folding of proteins