Studies of Pseudomonas aeruginosa azurin mutants: Cavities in β-barrel do not affect refolding speed

Biophysical Journal

Volumn 82, Issue 5, 2002, Pages 2645-2651

  Pozdnyakova, Irina ^a   Guidry, Jesse ^a   Wittung Stafshede, Pernilla ^a  

^a Tulane University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APOPROTEIN; AZURIN; COPPER PROTEIN; MUTANT PROTEIN;

ARTICLE; CHEMICAL REACTION; HYDROPHOBICITY; KINETICS; NONHUMAN; PROTEIN FOLDING; PSEUDOMONAS AERUGINOSA; REACTION ANALYSIS; THERMODYNAMICS; THERMOSTABILITY;

BACTERIA (MICROORGANISMS); NEGIBACTERIA; PSEUDOMONAS; PSEUDOMONAS AERUGINOSA;

EID: 0036225868     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(02)75606-3     Document Type: Article

References (27)

1. Copper protein structures
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3. Kinetic studies of beta-sheet protein folding
4. Folding of beta-sheet proteins
5. Resonance Raman spectroscopy of the azurin His117Gly mutant: Interconversion of type 1 and type 2 copper sites through exogenous ligands
6. Fast events in protein folding
7. Nucleation mechanisms in protein folding
8. Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism
9. Rate of beta-structure formation in polypeptides
10. Unique environment of Trp48 in Pseudomonas aeruginosa azurin as probed by site-directed mutagenesis and dynamic fluorescence spectroscopy
11. The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology
12. Crystal structures of modified apo-Hisl17Gly and apo-His46Gly mutants of Pseudomonas aeruginosa azurin
13. How do small single-domain proteins fold?
14. The structural role of the copper-coordinating and surface-exposed histidine residue in the blue copper protein azurin
15. Expression of the blue copper protein azurin from Pseudomonas aeruginosa in Escherichia coli
16. The effect of the metal ion on the folding energetics of azurin: A comparison of the native, zinc and apoprotein
17. Characterization and crystal structure of zinc azurin, a by-product of heterologous expression in Escherichia coli of Pseudomonas aeruginosa copper azurin
18. Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85 A resolution
19. The stability of globular proteins
20. Contact order, transition state placement and the refolding rates of single domain proteins
21. Copper triggered b-hairpin formation: Initiation site for azurin folding?
22. Copper stabilizes azurin by decreasing the unfolding rate
23. Probing copper ligands in denatured Pseudomonas aeruginosa azurin: Unfolding His117Gly and His46Gly mutants
24. Effect of preformed correct tertiary interactions on rapid two-state tendamistat folding: Evidence for hairpins as initiation sites for beta-sheet formation
25. Contribution of water molecules in the interior of a protein to the conformational stability
26. Protein denaturation: C. Theoretical models for the mechanism of denaturation
27. Spectroscopic and mechanistic studies of type-1 and type-2 copper sites in Pseudomonas aeruginosa azurin as obtained by addition of external ligands to mutant His46Gly