Kinetics of interaction of partially folded proteins with a hydrophobic dye: Evidence that molten globule character is maximal in early folding intermediates

Protein Science

Volumn 4, Issue 8, 1995, Pages 1553-1562

  Engelhard, Markus ^a   Evans, Philip A ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

8 anilino 1 naphthalenesulfonate; carbonic anhydrase; folding intermediate; molten globule; protein folding; stopped flow; lactalbumin

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ALPHA LACTALBUMIN; CARBONATE DEHYDRATASE; GLOBULAR PROTEIN;

ARTICLE; CONFORMATIONAL TRANSITION; FLUORESCENCE; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN FOLDING; PROTEIN STABILITY;

ANILINO NAPHTHALENESULFONATES; ANIMAL; CARBONIC ANHYDRASES; CATTLE; FLUORESCENT DYES; HUMAN; KINETICS; LACTALBUMIN; PROTEIN FOLDING; SUPPORT, NON-U.S. GOV'T;

EID: 0029115374     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.5560040813     Document Type: Article

References (26)

1. Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig α‐lactalbumin
2. Kinetic resolution of peptide bond and sidechain far‐UV circular dichroism during the folding of hen egg white lysozyme
3. The native state of apomyoglobin described by proton NMR spectroscopy: Interaction with the paramagnetic probe HyTEMPO and the fluorescent dye ANS
4. Compact state of a protein with pronounced small scale mobility: Bovine α‐lactalbumin
5. Probing the structure of folding intermediates
6. 2 subunit is a “molten globule.”
7. Tertiary interactions in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probes
8. Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time‐resolved fluorescence spectroscopy
9. Development of nonpolar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by l‐anilinonaphthalene‐8‐sulfonate binding
10. Intermediates in the folding reactions of small proteins
11. Rapid formation of secondary structure framework in protein folding studied by stopped‐flow circular dichroism
12. Kinetic circular‐dichroism shows that the S‐peptide α‐helix of ribonuclease‐S unfolds fast and refolds slowly
13. Structure and stability of an early folding intermediate of Escherichia coli trp aporepressor measured by far‐UV stopped flow circular dichroism and 8‐anilino‐1‐naphthalene sulfonate binding
14. Pathways of protein folding
15. Purification and separation of holo‐forms and apo‐forms of Saccharopolyspora erythraea acyl‐carrier protein released from recombinant Escherichia coli by freezing and thawing
16. Binding of naphthalene dyes to the N and A conformers of bovine α‐lactalbumin
17. Kinetic studies on binding of bovine serum albumin with 1‐anilino‐8‐naphthalene sulfonate
18. Evidence for a molten globule state as a general intermediate in protein folding
19. Diffusion‐controlled association of a dye, 1‐anilinonaphthalene‐8‐sulfonic acid, to a protein, bovine serum albumin, using a fast‐flow microsecond mixer and stopped‐flow
20. Sequential mechanism of refolding of carbonic anhydrase B
21. Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe
22. Protein engineering and the dissection of protein folding pathways
23. Protein conformational changes induced by 1,1′‐bis(4‐anilino‐5‐naphthalenesulfonic acid): Preferential binding to the molten globule of DnaK
24. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin
25. Reversible folding of rhodanese
26. Folding of the phage P22 coat protein in vitro