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Journal Abstract Search

219 related items for PubMed ID: 17512540

  • 1. Kinetic isotope effects reveal the presence of significant secondary structure in the transition state for the folding of the N-terminal domain of L9.
    Sato S, Raleigh DP.
    J Mol Biol; 2007 Jul 06; 370(2):349-55. PubMed ID: 17512540
    [Abstract] [Full Text] [Related]

  • 2. D/H amide kinetic isotope effects reveal when hydrogen bonds form during protein folding.
    Krantz BA, Moran LB, Kentsis A, Sosnick TR.
    Nat Struct Biol; 2000 Jan 06; 7(1):62-71. PubMed ID: 10625430
    [Abstract] [Full Text] [Related]

  • 3. Amide backbone and water-related H/D isotope effects on the dynamics of a protein folding reaction.
    Parker MJ, Clarke AR.
    Biochemistry; 1997 May 13; 36(19):5786-94. PubMed ID: 9153419
    [Abstract] [Full Text] [Related]

  • 4. Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology.
    Li Y, Gupta R, Cho JH, Raleigh DP.
    Biochemistry; 2007 Jan 30; 46(4):1013-21. PubMed ID: 17240985
    [Abstract] [Full Text] [Related]

  • 5. Understanding protein hydrogen bond formation with kinetic H/D amide isotope effects.
    Krantz BA, Srivastava AK, Nauli S, Baker D, Sauer RT, Sosnick TR.
    Nat Struct Biol; 2002 Jun 30; 9(6):458-63. PubMed ID: 11979278
    [Abstract] [Full Text] [Related]

  • 6. pH-dependent stability and folding kinetics of a protein with an unusual alpha-beta topology: the C-terminal domain of the ribosomal protein L9.
    Sato S, Raleigh DP.
    J Mol Biol; 2002 Apr 26; 318(2):571-82. PubMed ID: 12051860
    [Abstract] [Full Text] [Related]

  • 7. 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]

  • 8. pH-dependent interactions and the stability and folding kinetics of the N-terminal domain of L9. Electrostatic interactions are only weakly formed in the transition state for folding.
    Luisi DL, Raleigh DP.
    J Mol Biol; 2000 Jun 16; 299(4):1091-100. PubMed ID: 10843860
    [Abstract] [Full Text] [Related]

  • 9. Direct analysis of backbone-backbone hydrogen bond formation in protein folding transition states.
    Yang X, Wang M, Fitzgerald MC.
    J Mol Biol; 2006 Oct 20; 363(2):506-19. PubMed ID: 16963082
    [Abstract] [Full Text] [Related]

  • 10. Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9.
    Kuhlman B, Luisi DL, Evans PA, Raleigh DP.
    J Mol Biol; 1998 Dec 18; 284(5):1661-70. PubMed ID: 9878377
    [Abstract] [Full Text] [Related]

  • 11. Use of the novel fluorescent amino acid p-cyanophenylalanine offers a direct probe of hydrophobic core formation during the folding of the N-terminal domain of the ribosomal protein L9 and provides evidence for two-state folding.
    Aprilakis KN, Taskent H, Raleigh DP.
    Biochemistry; 2007 Oct 30; 46(43):12308-13. PubMed ID: 17924662
    [Abstract] [Full Text] [Related]

  • 12. Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing.
    Anil B, Sato S, Cho JH, Raleigh DP.
    J Mol Biol; 2005 Dec 02; 354(3):693-705. PubMed ID: 16246369
    [Abstract] [Full Text] [Related]

  • 13. Thermodynamics and kinetics of non-native interactions in protein folding: a single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state.
    Cho JH, Sato S, Raleigh DP.
    J Mol Biol; 2004 May 07; 338(4):827-37. PubMed ID: 15099748
    [Abstract] [Full Text] [Related]

  • 14. The unfolded state of NTL9 is compact in the absence of denaturant.
    Anil B, Li Y, Cho JH, Raleigh DP.
    Biochemistry; 2006 Aug 22; 45(33):10110-6. PubMed ID: 16906769
    [Abstract] [Full Text] [Related]

  • 15. Analysis of the pH-dependent folding and stability of histidine point mutants allows characterization of the denatured state and transition state for protein folding.
    Horng JC, Cho JH, Raleigh DP.
    J Mol Biol; 2005 Jan 07; 345(1):163-73. PubMed ID: 15567419
    [Abstract] [Full Text] [Related]

  • 16. 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]

  • 17. Conformational plasticity in folding of the split beta-alpha-beta protein S6: evidence for burst-phase disruption of the native state.
    Otzen DE, Oliveberg M.
    J Mol Biol; 2002 Apr 05; 317(4):613-27. PubMed ID: 11955013
    [Abstract] [Full Text] [Related]

  • 18. Amide proton exchange measurements as a probe of the stability and dynamics of the N-terminal domain of the ribosomal protein L9: comparison with the intact protein.
    Vugmeyster L, Kuhlman B, Raleigh DP.
    Protein Sci; 1998 Sep 05; 7(9):1994-7. PubMed ID: 9761480
    [Abstract] [Full Text] [Related]

  • 19. pH dependent thermodynamic and amide exchange studies of the C-terminal domain of the ribosomal protein L9: implications for unfolded state structure.
    Li Y, Horng JC, Raleigh DP.
    Biochemistry; 2006 Jul 18; 45(28):8499-506. PubMed ID: 16834323
    [Abstract] [Full Text] [Related]

  • 20. The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State.
    Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP.
    Biophys J; 2017 May 09; 112(9):1797-1806. PubMed ID: 28494951
    [Abstract] [Full Text] [Related]

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