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109 related items for PubMed ID: 9761480

  • 1. 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; 7(9):1994-7. PubMed ID: 9761480
    [Abstract] [Full Text] [Related]

  • 2. Structure and stability of the N-terminal domain of the ribosomal protein L9: evidence for rapid two-state folding.
    Kuhlman B, Boice JA, Fairman R, Raleigh DP.
    Biochemistry; 1998 Jan 27; 37(4):1025-32. PubMed ID: 9454593
    [Abstract] [Full Text] [Related]

  • 3. 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]

  • 4. Folding of the multidomain ribosomal protein L9: the two domains fold independently with remarkably different rates.
    Sato S, Kuhlman B, Wu WJ, Raleigh DP.
    Biochemistry; 1999 Apr 27; 38(17):5643-50. PubMed ID: 10220353
    [Abstract] [Full Text] [Related]

  • 5. On the relationship between protein stability and folding kinetics: a comparative study of the N-terminal domains of RNase HI, E. coli and Bacillus stearothermophilus L9.
    Sato S, Xiang S, Raleigh DP.
    J Mol Biol; 2001 Sep 21; 312(3):569-77. PubMed ID: 11563917
    [Abstract] [Full Text] [Related]

  • 6. 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]

  • 7. 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]

  • 8. The stability and dynamics of ribosomal protein L9: investigations of a molecular strut by amide proton exchange and circular dichroism.
    Lillemoen J, Cameron CS, Hoffman DW.
    J Mol Biol; 1997 May 02; 268(2):482-93. PubMed ID: 9159485
    [Abstract] [Full Text] [Related]

  • 9. An exceptionally stable helix from the ribosomal protein L9: implications for protein folding and stability.
    Kuhlman B, Yang HY, Boice JA, Fairman R, Raleigh DP.
    J Mol Biol; 1997 Aug 01; 270(5):640-7. PubMed ID: 9245593
    [Abstract] [Full Text] [Related]

  • 10. Effects of varying the local propensity to form secondary structure on the stability and folding kinetics of a rapid folding mixed alpha/beta protein: characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9.
    Luisi DL, Kuhlman B, Sideras K, Evans PA, Raleigh DP.
    J Mol Biol; 1999 May 28; 289(1):167-74. PubMed ID: 10339414
    [Abstract] [Full Text] [Related]

  • 11. 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]

  • 12. Global analysis of the thermal and chemical denaturation of the N-terminal domain of the ribosomal protein L9 in H2O and D2O. Determination of the thermodynamic parameters, deltaH(o), deltaS(o), and deltaC(o)p and evaluation of solvent isotope effects.
    Kuhlman B, Raleigh DP.
    Protein Sci; 1998 Nov 30; 7(11):2405-12. PubMed ID: 9828007
    [Abstract] [Full Text] [Related]

  • 13. Conformational analysis of a set of peptides corresponding to the entire primary sequence of the N-terminal domain of the ribosomal protein L9: evidence for stable native-like secondary structure in the unfolded state.
    Luisi DL, Wu WJ, Raleigh DP.
    J Mol Biol; 1999 Mar 26; 287(2):395-407. PubMed ID: 10080901
    [Abstract] [Full Text] [Related]

  • 14. 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]

  • 15. pKa values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions.
    Kuhlman B, Luisi DL, Young P, Raleigh DP.
    Biochemistry; 1999 Apr 13; 38(15):4896-903. PubMed ID: 10200179
    [Abstract] [Full Text] [Related]

  • 16. The native state conformational ensemble of the SH3 domain from alpha-spectrin.
    Sadqi M, Casares S, Abril MA, López-Mayorga O, Conejero-Lara F, Freire E.
    Biochemistry; 1999 Jul 13; 38(28):8899-906. PubMed ID: 10413463
    [Abstract] [Full Text] [Related]

  • 17. An investigation of the dynamics of ribosomal protein L9 using heteronuclear NMR relaxation measurements.
    Lillemoen J, Hoffman DW.
    J Mol Biol; 1998 Aug 21; 281(3):539-51. PubMed ID: 9698568
    [Abstract] [Full Text] [Related]

  • 18. 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]

  • 19. pH jump studies of the folding of the multidomain ribosomal protein L9: the structural organization of the N-terminal domain does not affect the anomalously slow folding of the C-terminal domain.
    Sato S, Luisi DL, Raleigh DP.
    Biochemistry; 2000 Apr 25; 39(16):4955-62. PubMed ID: 10769155
    [Abstract] [Full Text] [Related]

  • 20. Direct characterization of the folded, unfolded and urea-denatured states of the C-terminal domain of the ribosomal protein L9.
    Li Y, Picart F, Raleigh DP.
    J Mol Biol; 2005 Jun 17; 349(4):839-46. PubMed ID: 15890362
    [Abstract] [Full Text] [Related]

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