A simple way to measure protein refolding rates in water

Journal of Molecular Biology

Volumn 313, Issue 3, 2001, Pages 479-483

  Otzen, Daniel E ^a   Oliveberg, Mikael ^b  

^a AALBORG UNIVERSITY   (Denmark)

^b UMEÅ UNIVERSITY   (Sweden)

Author keywords

Chevron plots; Cyclodextrin; Protein folding; SDS; Stopped flow

Indexed keywords

ALPHA CYCLODEXTRIN; BUFFER; DODECYL SULFATE SODIUM; WATER;

ARTICLE; DILUTION; HEN; MEASUREMENT; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN FOLDING;

EID: 0035955556     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5039     Document Type: Article

References (24)

1. An integrated kinetic analysis of intermediates and transition states in protein folding reactions
2. Structural changes in the transition state of protein folding: An alternative interpretation of curved chevron plots
3. Folding of Chymotrypsin Inhibitor 2. 1: Evidence for a two-state transition
4. A new approach to the study of transient protein conformations: The formation of a semi-buried salt link in the folding pathway of barnase
5. Acid-induced folding of proteins
6. Neutron diffraction f α, β and γ cyzlodextrins: Hydrogen bonding patterns
7. Microcalorimetric titration of α-cyclodextrin with some straight-chain alkan-1-ols at 288.15, 298.15 and 308.15 K
8. Thermodynamics of molecular recognition by cyclodextrins. 1. Calorimetric titration of inclusion complexation of naphthalenesulfonates with α-, β- and γ-cyclodextrins: Enthalpy-entropy compensation
9. Microcalorimetric titration of α-cyclodextrin with some straight-chain α,ω-dicarboxylates in aqueous solution at different temperatures
10. Artificial chaperone-assisted refolding of denatured-reduced lysozyme: Modulation of the competition between renaturation and aggregation
11. Artificial chaperone-assisted refolding of carbonic anhydrase B
12. Refolding of SDS-and thermally denatured MM-creatine kinase using cyclodextrins
13. Mechanistic comparison of artificial-chaperone-assisted and unassisted refolding of urea-denatured carbonic anhydrase B
14. Upper limit of the timescale for diffusion and chain collapse in chymotrypsin inhibitor 2
15. Tertiary interactions in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probes
16. Salt-induced detour through compact regions of the protein folding landscape
17. Inclusion compounds. XIX. The formation of inclusion compounds of α-cyclodextrin in aqueous solutions. Thermodynamics and kinetics
18. Cyclodextrin Technology
19. Interaction of L-tryptophan with α-cyclodextrin: Studies with calorimetry and protein NMR
20. Estimation of the pH-independent binding constants of alanylphenylalanine and leucylphenylalanine steroisomers with β-cyclodextrin in the presence of urea
21. Folding of Chymotrypsin Inhibitor 2.2: Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding
22. The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of CI2
23. Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2
24. Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation