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Journal Abstract Search

139 related items for PubMed ID: 10339414

  • 1. 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]

  • 2. 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
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  • 3. 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
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  • 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
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  • 5. 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
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  • 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
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  • 10. 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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  • 11. 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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  • 12. 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 18; 7(9):1994-7. PubMed ID: 9761480
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  • 13. Conformational analysis of peptide fragments derived from the peripheral subunit-binding domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: evidence for nonrandom structure in the unfolded state.
    Spector S, Rosconi M, Raleigh DP.
    Biopolymers; 1999 Jan 18; 49(1):29-40. PubMed ID: 10070261
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  • 14. Characterization of large peptide fragments derived from the N-terminal domain of the ribosomal protein L9: definition of the minimum folding motif and characterization of local electrostatic interactions.
    Horng JC, Moroz V, Rigotti DJ, Fairman R, Raleigh DP.
    Biochemistry; 2002 Nov 12; 41(45):13360-9. PubMed ID: 12416980
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  • 15. A tale of two secondary structure elements: when a beta-hairpin becomes an alpha-helix.
    Cregut D, Civera C, Macias MJ, Wallon G, Serrano L.
    J Mol Biol; 1999 Sep 17; 292(2):389-401. PubMed ID: 10493883
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  • 16. 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]

  • 17. Involvement of the N- and C-terminal fragments of bovine pancreatic deoxyribonuclease in active protein folding.
    Chen WJ, Huang PT, Liu J, Liao TH.
    Biochemistry; 2004 Aug 24; 43(33):10653-63. PubMed ID: 15311926
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  • 19. Stability and folding kinetics of a ubiquitin mutant with a strong propensity for nonnative beta-hairpin conformation in the unfolded state.
    Platt GW, Simpson SA, Layfield R, Searle MS.
    Biochemistry; 2003 Nov 25; 42(46):13762-71. PubMed ID: 14622023
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  • 20. A minimum folding unit in the ankyrin repeat protein p16(INK4).
    Zhang B, Peng Zy.
    J Mol Biol; 2000 Jun 16; 299(4):1121-32. PubMed ID: 10843863
    [Abstract] [Full Text] [Related]

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