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283 related items for PubMed ID: 8951383

  • 1. Titration properties and thermodynamics of the transition state for folding: comparison of two-state and multi-state folding pathways.
    Tan YJ, Oliveberg M, Fersht AR.
    J Mol Biol; 1996 Nov 29; 264(2):377-89. PubMed ID: 8951383
    [Abstract] [Full Text] [Related]

  • 2. The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding.
    Itzhaki LS, Otzen DE, Fersht AR.
    J Mol Biol; 1995 Nov 24; 254(2):260-88. PubMed ID: 7490748
    [Abstract] [Full Text] [Related]

  • 3. The changing nature of the protein folding transition state: implications for the shape of the free-energy profile for folding.
    Oliveberg M, Tan YJ, Silow M, Fersht AR.
    J Mol Biol; 1998 Apr 10; 277(4):933-43. PubMed ID: 9545382
    [Abstract] [Full Text] [Related]

  • 4. The nature of the free energy barriers to two-state folding.
    Akmal A, Muñoz V.
    Proteins; 2004 Oct 01; 57(1):142-52. PubMed ID: 15326600
    [Abstract] [Full Text] [Related]

  • 5. Thermodynamics of transient conformations in the folding pathway of barnase: reorganization of the folding intermediate at low pH.
    Oliveberg M, Fersht AR.
    Biochemistry; 1996 Feb 27; 35(8):2738-49. PubMed ID: 8611580
    [Abstract] [Full Text] [Related]

  • 6. Conversion of two-state to multi-state folding kinetics on fusion of two protein foldons.
    Inaba K, Kobayashi N, Fersht AR.
    J Mol Biol; 2000 Sep 08; 302(1):219-33. PubMed ID: 10964571
    [Abstract] [Full Text] [Related]

  • 7. Folding pathway of FKBP12 and characterisation of the transition state.
    Main ER, Fulton KF, Jackson SE.
    J Mol Biol; 1999 Aug 13; 291(2):429-44. PubMed ID: 10438630
    [Abstract] [Full Text] [Related]

  • 8. Folding of circular and permuted chymotrypsin inhibitor 2: retention of the folding nucleus.
    Otzen DE, Fersht AR.
    Biochemistry; 1998 Jun 02; 37(22):8139-46. PubMed ID: 9609709
    [Abstract] [Full Text] [Related]

  • 9. The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2.
    Tan YJ, Oliveberg M, Otzen DE, Fersht AR.
    J Mol Biol; 1997 Jun 20; 269(4):611-22. PubMed ID: 9217264
    [Abstract] [Full Text] [Related]

  • 10. Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2.
    Lopez-Hernandez E, Serrano L.
    Fold Des; 1995 Jun 20; 1(1):43-55. PubMed ID: 9162138
    [Abstract] [Full Text] [Related]

  • 11. Kinetic analysis of molecular dynamics simulations reveals changes in the denatured state and switch of folding pathways upon single-point mutation of a beta-sheet miniprotein.
    Muff S, Caflisch A.
    Proteins; 2008 Mar 20; 70(4):1185-95. PubMed ID: 17847092
    [Abstract] [Full Text] [Related]

  • 12. Search for nucleation sites in smaller fragments of chymotrypsin inhibitor 2.
    Itzhaki LS, Neira JL, Ruiz-Sanz J, de Prat Gay G, Fersht AR.
    J Mol Biol; 1995 Nov 24; 254(2):289-304. PubMed ID: 7490749
    [Abstract] [Full Text] [Related]

  • 13. Folding of horse cytochrome c in the reduced state.
    Bhuyan AK, Udgaonkar JB.
    J Mol Biol; 2001 Oct 05; 312(5):1135-60. PubMed ID: 11580255
    [Abstract] [Full Text] [Related]

  • 14. Perturbed pKA-values in the denatured states of proteins.
    Tan YJ, Oliveberg M, Davis B, Fersht AR.
    J Mol Biol; 1995 Dec 15; 254(5):980-92. PubMed ID: 7500365
    [Abstract] [Full Text] [Related]

  • 15. Thermodynamic properties of an extremely rapid protein folding reaction.
    Schindler T, Schmid FX.
    Biochemistry; 1996 Dec 24; 35(51):16833-42. PubMed ID: 8988022
    [Abstract] [Full Text] [Related]

  • 16. Structure of the transition state for folding of a protein derived from experiment and simulation.
    Daggett V, Li A, Itzhaki LS, Otzen DE, Fersht AR.
    J Mol Biol; 1996 Mar 29; 257(2):430-40. PubMed ID: 8609634
    [Abstract] [Full Text] [Related]

  • 17. Electrostatic interactions in the denatured state and in the transition state for protein folding: effects of denatured state interactions on the analysis of transition state structure.
    Cho JH, Raleigh DP.
    J Mol Biol; 2006 Jun 23; 359(5):1437-46. PubMed ID: 16787780
    [Abstract] [Full Text] [Related]

  • 18. Movement of the position of the transition state in protein folding.
    Matouschek A, Otzen DE, Itzhaki LS, Jackson SE, Fersht AR.
    Biochemistry; 1995 Oct 17; 34(41):13656-62. PubMed ID: 7577956
    [Abstract] [Full Text] [Related]

  • 19.
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  • 20. The folding pathway of ubiquitin from all-atom molecular dynamics simulations.
    Marianayagam NJ, Jackson SE.
    Biophys Chem; 2004 Oct 01; 111(2):159-71. PubMed ID: 15381313
    [Abstract] [Full Text] [Related]

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