Native hydrogen bonds in a molten globule: The apoflavodoxin thermal intermediate

Journal of Molecular Biology

Volumn 306, Issue 4, 2001, Pages 877-888

  Irún, María P ^a   Garcia Mira, Maria M ^b   Sanchez Ruiz, Jose M ^b   Sancho, Javier ^a  

^a UNIVERSITY OF ZARAGOZA   (Spain)

^b UNIVERSITY OF GRANADA   (Spain)

Author keywords

Hydrogen bond; Molten globule; Protein folding; Protein intermediate; Protein stability

Indexed keywords

FLAVODOXIN;

ANABAENA; ARTICLE; CONFORMATIONAL TRANSITION; ENERGY TRANSFER; ENTHALPY; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY;

ANABAENA; NOSTOC SP. PCC 7119;

EID: 0035793715     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4436     Document Type: Article

References (47)

1. Principles of protein stability derived from protein engineering experiments
2. Engineering enzymes for stability
3. Forces contributing to the conformational stability of proteins
4. Protein stability: Still an unsolved problem
5. Protein folding: From the Levinthal paradox to structure prediction
6. Enhanced protein thermostability from designed mutations that interact with α-helix dipoles
7. Substantial increase of protein stability by multiple disulphide bonds
8. Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive
9. Design and structural analysis of an engineered thermostable chicken lysozyme
10. Stabilization of proteins by rational design of alpha-helix stability using helix/coil transition theory
11. Structural and mutagenesis studies of leishmania triosephosphate isomerase: A point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power
12. Increasing protein stability by altering long-range Coulombic interactions
13. Engineering a thermostable protein via optimisation of charge-charge interactions in the protein surface
14. Kinetic role of early intermediates in protein folding
15. The molten globule state
16. Navigating the folding routes
17. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
18. Following protein folding in real time using NMR spectroscopy
19. The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
20. Amyloid fibril formation by an SH3 domain
21. A specific hydrophobic core in the alpha-lactalbumin molten globule
22. Intrinsic stability of individual alpha helices modulates structure and stability of the apomyoglobin molten globule form
23. Effects of amino acid substitutions in the hydrophobic core of alpha-lactalbumin on the stability of the molten globule state
24. Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate
25. Contribution of individual residues to formation of the native-like tertiary topology in the alpha-lactalbumin molten globule
26. Native tertiary structure in an A-state
27. Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of protein's overall topology
28. Packing interactions in the apomyoglobin folding intermediate
29. Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations
30. The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure
31. Isolation and overexpression in Escherichia coli of the flavodoxin gene from Anabæna PCC 7119
32. Closure of a tyrosine/tryptophan aromatic gate leads to a compact fold in apoflavodoxin
33. Apoflavodoxin: Structure, stability, and FMN binding
34. Conformational stability of apoflavodoxin
35. Cooperative stabilisation of a molten globule apoflavodoxin fragment
36. Energetics of a hydrogen bond (charged and neutral) and of a cation-π interaction in apoflavodoxin
37. Dissecting the energetics of the apoflavodoxin-FMN complex
38. The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate
39. Differential scanning calorimetry of proteins
40. A new ultrasensitive scanning calorimeter
41. Detection of a stable intermediate in the thermal unfolding of a cysteine-free form of dihydrofolate reductase from Escherichia coli
42. The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
43. Mapping transition states of protein unfolding by protein engineering of ligand-binding sites
44. Site-directed mutagenesis of virtually any plasmid by eliminating a unique site
45. Chemical and physical characterisation of the Shethna flavoprotein and kinetics and thermodynamics of flavin analogue binding to the apoprotein
46. Measuring the conformational stability of a protein
47. Cold denaturation of ubiquitin