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349 related items for PubMed ID: 9828007

  • 1. 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; 7(11):2405-12. PubMed ID: 9828007
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  • 2. Thermal and urea-induced unfolding of the marginally stable lac repressor DNA-binding domain: a model system for analysis of solute effects on protein processes.
    Felitsky DJ, Record MT.
    Biochemistry; 2003 Feb 25; 42(7):2202-17. PubMed ID: 12590610
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  • 3. 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
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  • 4. 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
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  • 5. 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
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  • 8. Comparing the thermodynamic stabilities of a related thermophilic and mesophilic enzyme.
    Beadle BM, Baase WA, Wilson DB, Gilkes NR, Shoichet BK.
    Biochemistry; 1999 Feb 23; 38(8):2570-6. PubMed ID: 10029552
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  • 12. Thermodynamic analysis of catalysis by the dihydroorotases from hamster and Bacillus caldolyticus, as compared with the uncatalyzed reaction.
    Huang DT, Kaplan J, Menz RI, Katis VL, Wake RG, Zhao F, Wolfenden R, Christopherson RI.
    Biochemistry; 2006 Jul 11; 45(27):8275-83. PubMed ID: 16819826
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  • 14. Conformational and thermodynamic characterization of the molten globule state occurring during unfolding of cytochromes-c by weak salt denaturants.
    Qureshi SH, Moza B, Yadav S, Ahmad F.
    Biochemistry; 2003 Feb 18; 42(6):1684-95. PubMed ID: 12578383
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  • 16. 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
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  • 17. 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
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  • 19. Unfolding thermodynamics of Trp-cage, a 20 residue miniprotein, studied by differential scanning calorimetry and circular dichroism spectroscopy.
    Streicher WW, Makhatadze GI.
    Biochemistry; 2007 Mar 13; 46(10):2876-80. PubMed ID: 17295518
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  • 20. Thermodynamic characterization of the reversible, two-state unfolding of maltose binding protein, a large two-domain protein.
    Ganesh C, Shah AN, Swaminathan CP, Surolia A, Varadarajan R.
    Biochemistry; 1997 Apr 22; 36(16):5020-8. PubMed ID: 9125524
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