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Journal Abstract Search

209 related items for PubMed ID: 6355105

  • 41. Thermodynamics of maltose binding protein unfolding.
    Novokhatny V, Ingham K.
    Protein Sci; 1997 Jan; 6(1):141-6. PubMed ID: 9007986
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  • 44. The structure of D-galactose-binding protein at 4.1 A resolution looks like L-arabinose-binding protein.
    Quiocho FA, Pflugrath JW.
    J Biol Chem; 1980 Jul 25; 255(14):6559-51. PubMed ID: 6993475
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  • 47. Energetics of two-step binding of a chromophoric reaction product, trans-3-indoleacryloyl-CoA, to medium-chain acyl-coenzyme-A dehydrogenase.
    Qin L, Srivastava DK.
    Biochemistry; 1998 Mar 10; 37(10):3499-508. PubMed ID: 9521671
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  • 50. Thermodynamics of fatty acid binding to fatty acid-binding proteins and fatty acid partition between water and membranes measured using the fluorescent probe ADIFAB.
    Richieri GV, Ogata RT, Kleinfeld AM.
    J Biol Chem; 1995 Jun 23; 270(25):15076-84. PubMed ID: 7797491
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  • 51. A calorimetric study of peptide-phospholipid interactions: the glucagon-dimyristoylphosphatidylcholine complex.
    Epand RM, Sturtevant JM.
    Biochemistry; 1981 Aug 04; 20(16):4603-6. PubMed ID: 7295636
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  • 52. The conformational stability of the Streptomyces coelicolor histidine-phosphocarrier protein. Characterization of cold denaturation and urea-protein interactions.
    Neira JL, Gómez J.
    Eur J Biochem; 2004 Jun 04; 271(11):2165-81. PubMed ID: 15153107
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  • 54. Enthalpy and heat capacity changes for formation of an oligomeric DNA duplex: interpretation in terms of coupled processes of formation and association of single-stranded helices.
    Holbrook JA, Capp MW, Saecker RM, Record MT.
    Biochemistry; 1999 Jun 29; 38(26):8409-22. PubMed ID: 10387087
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  • 57. A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme.
    Connelly P, Ghosaini L, Hu CQ, Kitamura S, Tanaka A, Sturtevant JM.
    Biochemistry; 1991 Feb 19; 30(7):1887-91. PubMed ID: 1993203
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  • 59. Temperature dependence of the rate constants of the Escherichia coli RNA polymerase-lambda PR promoter interaction. Assignment of the kinetic steps corresponding to protein conformational change and DNA opening.
    Roe JH, Burgess RR, Record MT.
    J Mol Biol; 1985 Aug 05; 184(3):441-53. PubMed ID: 3900414
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