A comparison of the urea-induced unfolding of apoflavodoxin and flavodoxin from Desulfovibrio vulgaris

European Journal of Biochemistry

Volumn 269, Issue 1, 2002, Pages 212-223

  Nuallain, Brian Ó ^a,b   Mayhew, Stephen G ^a  

^a UNIVERSITY COLLEGE DUBLIN   (Ireland)

^b UNIVERSITY OF TENNESSEE MEDICAL CENTER   (United States)

Author keywords

Apoflavodoxin; Desulfovibrio vulgaris; Urea unfolding

Indexed keywords

AMINO ACID; APOFLAVODOXIN; APOPROTEIN; FLAVINE MONONUCLEOTIDE; FLAVODOXIN; FLAVOPROTEIN; ION; PHOSPHATE; SODIUM CHLORIDE; SODIUM DIHYDROGEN PHOSPHATE; UNCLASSIFIED DRUG; UREA;

AMINO ACID SEQUENCE; ARTICLE; CONCENTRATION RESPONSE; DESULFOVIBRIO VULGARIS; DISSOCIATION; EXPERIMENTAL MODEL; FLUORESCENCE; ION CURRENT; IONIC STRENGTH; KINETICS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; THERMODYNAMICS;

APOPROTEINS; DESULFOVIBRIO VULGARIS; FLAVIN MONONUCLEOTIDE; FLAVODOXIN; FLUORESCENCE; PROTEIN CONFORMATION; PROTEIN FOLDING; UREA;

DESULFOVIBRIO; DESULFOVIBRIO VULGARIS; NEGIBACTERIA;

EID: 0036156208     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.0014-2956.2002.02637.x     Document Type: Article

References (42)

1. Flavodoxins and electron-transferring flavoproteins
2. General properties of flavodoxins
3. Population statistics of protein structures: Lessons from structural classifications
4. Conformational stability of apoavodoxin
5. Cooperative stabilisation of a molten globule apoavodoxin fragment
6. The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate
7. Apoflavodoxin (un) folding followed at the residue level by NMR
8. Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: The flavodoxin story
9. Flavodoxin. Chemical and biological properties
10. No cofactor effect on equilibrium unfolding of Desulfovibrio desulfuricans flavodoxin
11. Comparison of the crystal structures of a flavodoxin in its three oxidation states at cryogenic temperatures
12. Crystal structure of flavodoxin from Desulfovibrio desulfuricans ATCC 27774 in two oxidation states
13. Redox and flavin-binding properties of recombinant flavodoxin from Desulfovibrio vulgaris (Hildenborough)
14. Fluorescence titration with apoflavodoxin: A sensitive assay for riboflavin 5′-phosphate and FAD in mixtures
15. A new method for preparing flavin-adenine dinucleotide
16. Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin
17. Determination and analysis of urea and guanidine hydrochloride denaturation curves
18. Unfolding free-energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
19. The energetics and cooperativity of protein folding: A simple experimental analysis based upon the solvation of internal residues
20. The solubility of amino acids and related compounds in aqueous urea solutions
21. The solubility of amino acids, diglycine, and triglycine in aqueous guanidine hydrochloride solutions
22. The stability of globular proteins
23. Non-polar group participation in the denaturation of proteins by 3 urea and guanidinium salts. Model compound studies
24. Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: The roles of ion association or release, screening, and ion effects on water activity
25. Fluorescence and the location of tryptophan residues in protein molecules
26. Protein denaturation. Part A and B
27. Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: Implications for redox potential regulation and flavodoxin folding
28. Analysis of protein structure by solution optical spectroscopy
29. Folding of chymotrypsin inhibitor 2. Evidence for a two-state transition
30. Protein interactions with urea and guanidinium chloride: A calorimetric study
31. Conformational stability of globular proteins
32. Thermodynamic analysis of the chemotactic protein from Escherichia coli CheY
33. Three-state analysis of sperm whale apomyoglobin folding
34. Kinetics and thermodynamics of the binding of riboflavin, riboflavin 5′-phosphate and riboflavin 3′,5′-bisphosphate by apoflavodoxins
35. X-ray crystal structure of the Desulfovibrio vulgaris (Hilden-borough) apoflavodoxin-riboflavin complex
36. Stabilisation of pancreatic ribonuclease against urea denaturation by anion binding
37. 1 is stabilised by cation and anion binding
38. The Hofmeister effect and the behaviour of water at interfaces
39. Primary sequence, oxidation-reduction potentials and tertiary-structure prediction of Desulfovibrio desulfuricans ATCC 27774 flavodoxin
40. Regulation of the redox potentials of flavodoxins: Modification of the flavin binding site