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146 related items for PubMed ID: 7749060

  • 1. Partial molar heat capacities and volumes of Gly-X-Gly tripeptides in aqueous solution: model studies for the rationalization of thermodynamic parameters of proteins.
    Vogl T, Hinz HJ, Hedwig GR.
    Biophys Chem; 1995 May; 54(3):261-9. PubMed ID: 7749060
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  • 2. A new set of peptide-based group heat capacities for use in protein stability calculations.
    Häckel M, Hinz HJ, Hedwig GR.
    J Mol Biol; 1999 Aug 06; 291(1):197-213. PubMed ID: 10438615
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  • 5. Group additivity schemes for the calculation of the partial molar heat capacities and volumes of unfolded proteins in aqueous solution.
    Hedwig GR, Hinz HJ.
    Biophys Chem; 2003 Aug 06; 100(1-3):239-60. PubMed ID: 12646369
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  • 8. Partial molar volumes of polypeptides and their constituent groups in aqueous solution over a broad temperature range.
    Makhatadze GI, Medvedkin VN, Privalov PL.
    Biopolymers; 1990 Aug 06; 30(11-12):1001-10. PubMed ID: 2081262
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  • 9. Amino acid side-chain contributions to free energy of transfer of tripeptides from water to octanol.
    Kim A, Szoka FC.
    Pharm Res; 1992 Apr 06; 9(4):504-14. PubMed ID: 1495896
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  • 10. Partial molar volumes of proteins: amino acid side-chain contributions derived from the partial molar volumes of some tripeptides over the temperature range 10-90 degrees C.
    Häckel M, Hinz HJ, Hedwig GR.
    Biophys Chem; 1999 Nov 15; 82(1):35-50. PubMed ID: 17030339
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  • 11. Partial molar heat capacities of the side chains of some amino acid residues in aqueous solution. The influence of the neighboring charges.
    Makhatadze GI, Gill SJ, Privalov PL.
    Biophys Chem; 1990 Oct 15; 38(1-2):33-7. PubMed ID: 17056435
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  • 12. Synthesis and folding of native collagen III model peptides.
    Henkel W, Vogl T, Echner H, Voelter W, Urbanke C, Schleuder D, Rauterberg J.
    Biochemistry; 1999 Oct 12; 38(41):13610-22. PubMed ID: 10521268
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  • 13. The role of cystine knots in collagen folding and stability, part I. Conformational properties of (Pro-Hyp-Gly)5 and (Pro-(4S)-FPro-Gly)5 model trimers with an artificial cystine knot.
    Barth D, Musiol HJ, Schütt M, Fiori S, Milbradt AG, Renner C, Moroder L.
    Chemistry; 2003 Aug 04; 9(15):3692-702. PubMed ID: 12898696
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  • 14. Interaction of 2,2,2-trifluoroethanol with proteins: calorimetric, densimetric and surface tension approach.
    Kundu A, Kishore N.
    Biophys Chem; 2004 Jun 01; 109(3):427-42. PubMed ID: 15110939
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  • 20. The observed change in heat capacity accompanying the thermal unfolding of proteins depends on the composition of the solution and on the method employed to change the temperature of unfolding.
    Liu Y, Sturtevant JM.
    Biochemistry; 1996 Mar 05; 35(9):3059-62. PubMed ID: 8608146
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