Comparison of the denaturant-induced unfolding of the bovine and human α-lactalbumin molten globules

Journal of Molecular Biology

Volumn 312, Issue 1, 2001, Pages 261-273

  Wijesinha Bettoni, Ramani ^a   Dobson, Christopher M ^a   Redfield, Christina ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Molten globule state; NMR; Protein folding; Urea unfolding; lactalbumin

Indexed keywords

ALPHA LACTALBUMIN; UREA;

ARTICLE; CATTLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; HUMAN; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY;

BOVINAE;

EID: 0035823118     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4927     Document Type: Article

References (51)

1. Stages in the mechanism of self-organization of protein molecules
2. Alpha-lactalbumin: Compact state with fluctuating tertiary structure?
3. Comparison of the transient folding intermediates in lysozyme and α-lactalbumin
4. Evidence for identity between the unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of α-lactalbumin and lysozyme
5. Rapid formation of a molten globule intermediate in refolding of α-lactalbumin
6. Structural characterization of a partly folded apomyoglobin intermediate
7. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
8. Molten-globule" state accumulates in carbonic anhydrase folding
9. Folding pathway of Escherichia coli ribonuclease HI: A circular dichroism, fluorescence, and NMR study
10. Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology
11. Inter- and intramolecular interactions of α-lactalbumin. III. Spectral changes at acid pH*
12. Compact state of a protein molecule with pronounced small-scale mobility - Bovine α-lactalbumin
13. The molten globule state as a clue for understanding the folding and cooperativity of globular protein structure
14. 1H NMR
15. Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig α-lactalbumin
16. A residue-specific NMR view of the non-cooperative unfolding of a molten globule
17. Structure and dynamics of the acid-denatured molten globule state of α-lactalbumin: A two-dimensional NMR study
18. Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human α-lactalbumin
19. Rapid collapse and slow structural reorganisation during the refolding of bovine α-lactalbumin
20. Structure and stability of the molten globule state of guinea-pig α-lactalbumin: A hydrogen exchange study
21. α-Lactalbumin forms a compact molten globule in the absence of disulfide bonds
22. The equilibrium folding pathway of staphylococcal nuclease: Identification of the most stable chain-chain interactions by NMR and CD spectroscopy
23. A dynamic bundle of four adjacent hydrophobic segments in the denatured state of staphylococcal nuclease
24. Protein folding for realists: A timeless phenomenon
25. Contribution of individual residues to formation of the native-like tertiary topology in the α-lactalbumin molten globule
26. A specific hydrophobic core in the α-lactalbumin molten globule
27. Bipartite structure of the α-lactalbumin molten globule
28. 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
29. Effects of amino acid substitutions in the hydrophobic core of α-lactalbumin on the stability of the molten globule state
30. Local and long-range interactions in the molten globule state: A study of chimeric proteins of bovine and human α-lactalbumin
31. Characterisation of protein unfolding by NMR diffusion measurements
32. Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partially folded bovine pancreatic trypsin inhibitor
33. The concept of a random coil. Residual structure in peptides and denatured proteins
34. Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea
35. A simple method for displaying the hydropathic character of a protein
36. Crystal structure of human α-lactalbumin at 1.7 Å resolution
37. Demonstration by NMR of folding domains in lysozyme
38. The folding of hen lysozyme involves partially structured intermediates and multiple pathways
39. The refolding of human lysozyme: A comparison with the structurally homologous hen lysozyme
40. Independent nucleation and heterogeneous assembly of structure during folding of equine lysozyme
41. Conservation of folding pathways in evolutionarily distant globin sequences
42. Critical role of beta-hairpin formation in protein G folding
43. Understanding protein folding via free-energy surfaces from theory and experiment
44. Study by mutagenesis of the roles of two aromatic clusters of alpha lactalbumin in aspects of its action in the lactose synthase system
45. Remarkable destabilization of recombinant alpha-lactalbumin by an extraneous N-terminal methionyl residue
46. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
47. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
48. −15N Hartmann-Hahn multiple quantum coherence and nuclear Overhauser multiple quantum coherence spectroscopy: Application to interleukin-1 β
49. Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
50. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures