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Journal Abstract Search


354 related items for PubMed ID: 15049688

  • 1. Kinetic role of helix caps in protein folding is context-dependent.
    Kapp GT, Richardson JS, Oas TG.
    Biochemistry; 2004 Apr 06; 43(13):3814-23. PubMed ID: 15049688
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  • 2. Rate-temperature relationships in lambda-repressor fragment lambda 6-85 folding.
    Yang WY, Gruebele M.
    Biochemistry; 2004 Oct 19; 43(41):13018-25. PubMed ID: 15476395
    [Abstract] [Full Text] [Related]

  • 3. Contribution of a buried hydrogen bond to lambda repressor folding kinetics.
    Myers JK, Oas TG.
    Biochemistry; 1999 May 25; 38(21):6761-8. PubMed ID: 10346896
    [Abstract] [Full Text] [Related]

  • 4. Folding kinetics of a fluorescent variant of monomeric lambda repressor.
    Ghaemmaghami S, Word JM, Burton RE, Richardson JS, Oas TG.
    Biochemistry; 1998 Jun 23; 37(25):9179-85. PubMed ID: 9636065
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  • 6. Helix-capping interaction in lambda Cro protein: a free energy simulation analysis.
    Tidor B.
    Proteins; 1994 Aug 23; 19(4):310-23. PubMed ID: 7984627
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  • 10. Relocation or duplication of the helix A sequence of T4 lysozyme causes only modest changes in structure but can increase or decrease the rate of folding.
    Sagermann M, Baase WA, Mooers BH, Gay L, Matthews BW.
    Biochemistry; 2004 Feb 10; 43(5):1296-301. PubMed ID: 14756565
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  • 15. Identification of native and non-native structure in kinetic folding intermediates of apomyoglobin.
    Nishimura C, Dyson HJ, Wright PE.
    J Mol Biol; 2006 Jan 06; 355(1):139-56. PubMed ID: 16300787
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  • 16. A calorimetric study of the folding-unfolding of an alpha-helix with covalently closed N and C-terminal loops.
    Taylor JW, Greenfield NJ, Wu B, Privalov PL.
    J Mol Biol; 1999 Aug 27; 291(4):965-76. PubMed ID: 10452900
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  • 17. Solution structure of the DNA-binding domain of NtrC with three alanine substitutions.
    Pelton JG, Kustu S, Wemmer DE.
    J Mol Biol; 1999 Oct 08; 292(5):1095-110. PubMed ID: 10512705
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  • 18. Importance of alpha-helix N-capping motif in stabilization of betabetaalpha fold.
    Koscielska-Kasprzak K, Cierpicki T, Otlewski J.
    Protein Sci; 2003 Jun 08; 12(6):1283-9. PubMed ID: 12761399
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  • 19. The dissociation rate of a winged helix protein-DNA complex is influenced by non-DNA contact residues.
    Shiyanova T, Liao X.
    Arch Biochem Biophys; 1999 Feb 15; 362(2):356-62. PubMed ID: 9989946
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  • 20. Folding at the speed limit.
    Yang WY, Gruebele M.
    Nature; 2003 May 08; 423(6936):193-7. PubMed ID: 12736690
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