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Journal Abstract Search

62 related items for PubMed ID: 2482748

  • 21. The conformational analysis of substance P analogs using high-field NMR techniques.
    Kawaki H, Otter A, Beierbeck H, Kotovych G, Stewart JM.
    J Biomol Struct Dyn; 1986 Feb; 3(4):795-803. PubMed ID: 2482046
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  • 24. Delineation of an active fragment and poly(L-proline) II conformation for candidacidal activity of bactenecin 5.
    Raj PA, Marcus E, Edgerton M.
    Biochemistry; 1996 Apr 09; 35(14):4314-25. PubMed ID: 8605180
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  • 26. Conformation and molecular dynamics calculations on uteroglobin fragment 18-47.
    Improta S, Pastore A, Mammi S, Peggion E.
    Biopolymers; 1994 Jun 09; 34(6):773-82. PubMed ID: 8025221
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  • 27. The solution conformations of ferrichrome and deferriferrichrome determined by 1H-NMR spectroscopy and computational modeling.
    Constantine KL, De Marco A, Madrid M, Brooks CL, Llinás M.
    Biopolymers; 1990 Jun 09; 30(3-4):239-56. PubMed ID: 2279065
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  • 29. Conformational study of the neurotensin and substance P fragments: Pro-Arg-Arg-Pro and Arg-Pro-Lys-Pro.
    Cotrait M.
    Int J Pept Protein Res; 1983 Jul 09; 22(1):110-8. PubMed ID: 6193076
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  • 30. Conformational behaviour of a cyclolinopeptide A analogue: two-dimensional NMR study of cyclo(Pro1-Pro-Phe-Phe-Ac6c-Ile-ala-Val8).
    Mazzeo M, Isernia C, Rossi F, Saviano M, Pedone C, Paolillo L, Benedetti E, Pavone V.
    J Pept Sci; 1995 Jul 09; 1(5):330-40. PubMed ID: 9223012
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  • 32. Method of modeling protein structure by the two-dimensional nuclear magnetic resonance spectroscopy data; application to the proteinase inhibitor BUSI IIA from bull seminal plasma.
    Sherman SA, Andrianov AM, Akhrem AA.
    J Biomol Struct Dyn; 1988 Feb 09; 5(4):785-801. PubMed ID: 3271489
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  • 35. Secondary structure of a herpes simplex virus glycoprotein D antigenic domain.
    Williamson MP, Handa BK, Hall MJ.
    Int J Pept Protein Res; 1986 May 09; 27(5):562-8. PubMed ID: 2426211
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  • 36. Two-dimensional 1H NMR study of a tetradecapeptide with the consensus sequence Arg5-Asp-Val-Arg-Gly9: structural effects of the outside substitution Ser12 by Ala12.
    Riand J, Chalaoux FR, Leseney AM, Baron D.
    J Biomol Struct Dyn; 1995 Apr 09; 12(5):993-1008. PubMed ID: 7626248
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  • 37. [Study of the spatial structure of des-Gly9-[Arg8]vasopressin by two-dimensional NMR spectroscopy and theoretical conformation analysis].
    Shenderovich MD, Sekatsis IP, Liepin'sh EE, Nikiforovich GV, Papsuevich OS.
    Bioorg Khim; 1985 Sep 09; 11(9):1180-91. PubMed ID: 4062995
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  • 40. A conformational study of Lys-Arg-Asp-Ser and analogs, a series of potent antithrombotic peptides. An approach based on simulated annealing and 1H NMR.
    Meddeb S, Demaret JP, Ballini JP, Fiat AM, Jollès P, Ptak M, Vigny P.
    J Biomol Struct Dyn; 1994 Apr 09; 11(5):959-81. PubMed ID: 7946066
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