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Journal Abstract Search

718 related items for PubMed ID: 11724558

  • 1. Conformational and dynamic characterization of the molten globule state of an apomyoglobin mutant with an altered folding pathway.
    Cavagnero S, Nishimura C, Schwarzinger S, Dyson HJ, Wright PE.
    Biochemistry; 2001 Dec 04; 40(48):14459-67. PubMed ID: 11724558
    [Abstract] [Full Text] [Related]

  • 2. Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobin.
    Cavagnero S, Dyson HJ, Wright PE.
    J Mol Biol; 1999 Jan 08; 285(1):269-82. PubMed ID: 9878405
    [Abstract] [Full Text] [Related]

  • 3. 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
    [Abstract] [Full Text] [Related]

  • 4. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin.
    Jennings PA, Wright PE.
    Science; 1993 Nov 05; 262(5135):892-6. PubMed ID: 8235610
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  • 5. NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding.
    Yao J, Chung J, Eliezer D, Wright PE, Dyson HJ.
    Biochemistry; 2001 Mar 27; 40(12):3561-71. PubMed ID: 11297422
    [Abstract] [Full Text] [Related]

  • 6. Probing the non-native H helix translocation in apomyoglobin folding intermediates.
    Aoto PC, Nishimura C, Dyson HJ, Wright PE.
    Biochemistry; 2014 Jun 17; 53(23):3767-80. PubMed ID: 24857522
    [Abstract] [Full Text] [Related]

  • 7. The kinetic and equilibrium molten globule intermediates of apoleghemoglobin differ in structure.
    Nishimura C, Dyson HJ, Wright PE.
    J Mol Biol; 2008 May 02; 378(3):715-25. PubMed ID: 18384808
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  • 9. Energetic frustration of apomyoglobin folding: role of the B helix.
    Nishimura C, Dyson HJ, Wright PE.
    J Mol Biol; 2010 Mar 12; 396(5):1319-28. PubMed ID: 20043917
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  • 10. Experimental studies of pathways of protein folding.
    Baldwin RL.
    Ciba Found Symp; 1991 Mar 12; 161():190-201; discussion 201-5. PubMed ID: 1667633
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  • 16. Stein and Moore Award address. The molten globule intermediate of apomyoglobin and the process of protein folding.
    Barrick D, Baldwin RL.
    Protein Sci; 1993 Jun 12; 2(6):869-76. PubMed ID: 8318892
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  • 17. Intrinsic stability of individual alpha helices modulates structure and stability of the apomyoglobin molten globule form.
    Kiefhaber T, Baldwin RL.
    J Mol Biol; 1995 Sep 08; 252(1):122-32. PubMed ID: 7666424
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  • 18. Molten globular characteristics of the native state of apomyoglobin.
    Lin L, Pinker RJ, Forde K, Rose GD, Kallenbach NR.
    Nat Struct Biol; 1994 Jul 08; 1(7):447-52. PubMed ID: 7664063
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  • 19. Changes in the apomyoglobin folding pathway caused by mutation of the distal histidine residue.
    Garcia C, Nishimura C, Cavagnero S, Dyson HJ, Wright PE.
    Biochemistry; 2000 Sep 19; 39(37):11227-37. PubMed ID: 10985768
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  • 20. Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations.
    Luo Y, Kay MS, Baldwin RL.
    Nat Struct Biol; 1997 Nov 19; 4(11):925-30. PubMed ID: 9360609
    [Abstract] [Full Text] [Related]

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