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Journal Abstract Search

220 related items for PubMed ID: 18227434

  • 21. Direct energy transfer to study the 3D structure of non-native proteins: AGH complex in molten globule state of apomyoglobin.
    Tcherkasskaya O, Ptitsyn OB.
    Protein Eng; 1999 Jun; 12(6):485-90. PubMed ID: 10388845
    [Abstract] [Full Text] [Related]

  • 22. Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR.
    Nishimura C.
    Proc Jpn Acad Ser B Phys Biol Sci; 2017 Jun; 93(1):10-27. PubMed ID: 28077807
    [Abstract] [Full Text] [Related]

  • 23. Loops linking secondary structure elements affect the stability of the molten globule intermediate state of apomyoglobin.
    Majorina MA, Balobanov VA, Uversky VN, Melnik BS.
    FEBS Lett; 2020 Oct; 594(20):3293-3304. PubMed ID: 32770670
    [Abstract] [Full Text] [Related]

  • 24. Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering.
    Kataoka M, Nishii I, Fujisawa T, Ueki T, Tokunaga F, Goto Y.
    J Mol Biol; 1995 May 26; 249(1):215-28. PubMed ID: 7776373
    [Abstract] [Full Text] [Related]

  • 25. Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for structural characterization by NMR.
    Eliezer D, Jennings PA, Dyson HJ, Wright PE.
    FEBS Lett; 1997 Nov 03; 417(1):92-6. PubMed ID: 9395082
    [Abstract] [Full Text] [Related]

  • 26. 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 03; 2(6):869-76. PubMed ID: 8318892
    [Abstract] [Full Text] [Related]

  • 27. Molten globule versus variety of intermediates: influence of anions on pH-denatured apomyoglobin.
    Tcherkasskaya O, Ptitsyn OB.
    FEBS Lett; 1999 Jul 23; 455(3):325-31. PubMed ID: 10437798
    [Abstract] [Full Text] [Related]

  • 28. Consequences of stabilizing the natively disordered f helix for the folding pathway of apomyoglobin.
    Nishimura C, Dyson HJ, Wright PE.
    J Mol Biol; 2011 Aug 05; 411(1):248-63. PubMed ID: 21640124
    [Abstract] [Full Text] [Related]

  • 29. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding.
    Eliezer D, Yao J, Dyson HJ, Wright PE.
    Nat Struct Biol; 1998 Feb 05; 5(2):148-55. PubMed ID: 9461081
    [Abstract] [Full Text] [Related]

  • 30. Noncooperative Formation of the off-pathway molten globule during folding of the alpha-beta parallel protein apoflavodoxin.
    Nabuurs SM, Westphal AH, van Mierlo CP.
    J Am Chem Soc; 2009 Feb 25; 131(7):2739-46. PubMed ID: 19170491
    [Abstract] [Full Text] [Related]

  • 31. Thermodynamic stability of the molten globule states of apomyoglobin.
    Nishii I, Kataoka M, Goto Y.
    J Mol Biol; 1995 Jul 07; 250(2):223-38. PubMed ID: 7608972
    [Abstract] [Full Text] [Related]

  • 32. Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings.
    Mohana-Borges R, Goto NK, Kroon GJ, Dyson HJ, Wright PE.
    J Mol Biol; 2004 Jul 23; 340(5):1131-42. PubMed ID: 15236972
    [Abstract] [Full Text] [Related]

  • 33. Structural origins of pH and ionic strength effects on protein stability. Acid denaturation of sperm whale apomyoglobin.
    Yang AS, Honig B.
    J Mol Biol; 1994 Apr 15; 237(5):602-14. PubMed ID: 8158640
    [Abstract] [Full Text] [Related]

  • 34. Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding.
    Nishii I, Kataoka M, Tokunaga F, Goto Y.
    Biochemistry; 1994 Apr 26; 33(16):4903-9. PubMed ID: 8161550
    [Abstract] [Full Text] [Related]

  • 35. Compactness of protein molten globules: temperature-induced structural changes of the apomyoglobin folding intermediate.
    Gast K, Damaschun H, Misselwitz R, Müller-Frohne M, Zirwer D, Damaschun G.
    Eur Biophys J; 1994 Apr 26; 23(4):297-305. PubMed ID: 7805629
    [Abstract] [Full Text] [Related]

  • 36. Interrupted hydrogen/deuterium exchange reveals the stable core of the remarkably helical molten globule of alpha-beta parallel protein flavodoxin.
    Nabuurs SM, van Mierlo CPM.
    J Biol Chem; 2010 Feb 05; 285(6):4165-4172. PubMed ID: 19959481
    [Abstract] [Full Text] [Related]

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  • 38. How Does Your Protein Fold? Elucidating the Apomyoglobin Folding Pathway.
    Dyson HJ, Wright PE.
    Acc Chem Res; 2017 Jan 17; 50(1):105-111. PubMed ID: 28032989
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