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425 related items for PubMed ID: 7799434

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  • 4. High helical propensity of the peptide fragments derived from beta-lactoglobulin, a predominantly beta-sheet protein.
    Hamada D, Kuroda Y, Tanaka T, Goto Y.
    J Mol Biol; 1995 Dec 08; 254(4):737-46. PubMed ID: 7500346
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  • 6. Fluoroalcohol-induced stabilization of the alpha-helical intermediates of lentil lectin: implication for non-hierarchical lectin folding.
    Naseem F, Khan RH.
    Arch Biochem Biophys; 2004 Nov 15; 431(2):215-23. PubMed ID: 15488470
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  • 9. Two-phase induction of the nonnative alpha-helical form of beta-lactoglobulin in the presence of trifluoroethanol.
    Mendieta J, Folqué H, Tauler R.
    Biophys J; 1999 Jan 15; 76(1 Pt 1):451-7. PubMed ID: 9876157
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  • 11. Conformational properties of four peptides spanning the sequence of hen lysozyme.
    Yang JJ, Buck M, Pitkeathly M, Kotik M, Haynie DT, Dobson CM, Radford SE.
    J Mol Biol; 1995 Sep 29; 252(4):483-91. PubMed ID: 7563067
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  • 14. Characterization of a trifluoroethanol-induced partially folded state of alpha-lactalbumin.
    Alexandrescu AT, Ng YL, Dobson CM.
    J Mol Biol; 1994 Jan 14; 235(2):587-99. PubMed ID: 8289283
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  • 15. Kinetic refolding of beta-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy.
    Arai M, Ikura T, Semisotnov GV, Kihara H, Amemiya Y, Kuwajima K.
    J Mol Biol; 1998 Jan 09; 275(1):149-62. PubMed ID: 9451446
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  • 16. Cooperative alpha-helix formation of beta-lactoglobulin induced by sodium n-alkyl sulfates.
    Chamani J, Moosavi-Movahedi AA, Rajabi O, Gharanfoli M, Momen-Heravi M, Hakimelahi GH, Neamati-Baghsiah A, Varasteh AR.
    J Colloid Interface Sci; 2006 Jan 01; 293(1):52-60. PubMed ID: 15996676
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  • 17. Alcohol-induced molten globule intermediates of proteins: are they real folding intermediates or off pathway products?
    Bhakuni V.
    Arch Biochem Biophys; 1998 Sep 15; 357(2):274-84. PubMed ID: 9735168
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  • 20. Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding.
    Taddei N, Chiti F, Fiaschi T, Bucciantini M, Capanni C, Stefani M, Serrano L, Dobson CM, Ramponi G.
    J Mol Biol; 2000 Jul 14; 300(3):633-47. PubMed ID: 10884358
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