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Volumn 865, Issue , 1998, Pages 37-44

Solution structure comparison of the VIP/PACAP family of peptides by NMR spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

HYPOPHYSIS ADENYLATE CYCLASE ACTIVATING POLYPEPTIDE; VASOACTIVE INTESTINAL POLYPEPTIDE;

EID: 0032419256     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.1998.tb11160.x     Document Type: Conference Paper
Times cited : (24)

References (17)
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    • Fournier, A., J. K. Saunders & S. St-Pierre. 1984. Synthesis, conformational studies and biological activities of VIP and related fragments. Peptides 5: 169-177.
    • (1984) Peptides , vol.5 , pp. 169-177
    • Fournier, A.1    Saunders, J.K.2    St-Pierre, S.3
  • 3
    • 0022980290 scopus 로고
    • Solution structure of human growth hormone releasing factor
    • Clore, G. M., S. R. Martin & A. M. Gronenborn. 1986. Solution structure of human growth hormone releasing factor. J. Mol. Biol. 191: 553-561.
    • (1986) J. Mol. Biol. , vol.191 , pp. 553-561
    • Clore, G.M.1    Martin, S.R.2    Gronenborn, A.M.3
  • 5
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    • Determination of the backbone conformation of secretin by restraint molecular dynamics on the basis of interproton distance data
    • Clore, G. M., M. Nilges, A. Brünger & A. M. Gronenborn. 1988. Determination of the backbone conformation of secretin by restraint molecular dynamics on the basis of interproton distance data. Eur. J. Biochem. 171: 479-484.
    • (1988) Eur. J. Biochem. , vol.171 , pp. 479-484
    • Clore, G.M.1    Nilges, M.2    Brünger, A.3    Gronenborn, A.M.4
  • 6
    • 0024535462 scopus 로고
    • Solution structure of an analogue of vasoactive intestinal peptide as determined by two-dimensional NMR and circular dichroism spectroscopies and constrained molecular dynamics
    • Fry, D. C., V. S. Madison, D. R. Bolin, D. N. Greeley, V. Toome & B. B. Wegrzynski. 1989. Solution structure of an analogue of vasoactive intestinal peptide as determined by two-dimensional NMR and circular dichroism spectroscopies and constrained molecular dynamics. Biochemistry 28: 2399-2409.
    • (1989) Biochemistry , vol.28 , pp. 2399-2409
    • Fry, D.C.1    Madison, V.S.2    Bolin, D.R.3    Greeley, D.N.4    Toome, V.5    Wegrzynski, B.B.6
  • 9
    • 0027315753 scopus 로고
    • Solution structure of pituitary adenylate cyclase activation polypeptide by nuclear magnetic resonance spectroscopy
    • Wray, V., C. Kakoschke, K. Nokihara & S. Naruse. 1993. Solution structure of pituitary adenylate cyclase activation polypeptide by nuclear magnetic resonance spectroscopy. Biochemistry 32 (No. 22): 5832-5841.
    • (1993) Biochemistry , vol.32 , Issue.22 , pp. 5832-5841
    • Wray, V.1    Kakoschke, C.2    Nokihara, K.3    Naruse, S.4
  • 10
    • 0028207562 scopus 로고
    • Structure of glucagon-like peptide(7-36) amide in a dodecylphosphocholine micelle as determined by 2D NMR
    • Thornton, K. & D. G. Gorenstein. 1994. Structure of glucagon-like peptide(7-36) amide in a dodecylphosphocholine micelle as determined by 2D NMR. Biochemistry 33: 3532-3539.
    • (1994) Biochemistry , vol.33 , pp. 3532-3539
    • Thornton, K.1    Gorenstein, D.G.2
  • 13
    • 0030292105 scopus 로고    scopus 로고
    • NMR study of five N-terminal peptide fragments of the vasoactive intestinal peptide: Crucial role of aromatic residues
    • Goossens, J.-F., P. Cotelle, P. Chavatte & J.-P. Hénichart. 1996. NMR study of five N-terminal peptide fragments of the vasoactive intestinal peptide: Crucial role of aromatic residues. Peptide Res. 9: 322-326.
    • (1996) Peptide Res. , vol.9 , pp. 322-326
    • Goossens, J.-F.1    Cotelle, P.2    Chavatte, P.3    Hénichart, J.-P.4
  • 14
    • 0029931971 scopus 로고    scopus 로고
    • NMR spectroscopic evidence that helodermin, unlike other members of the secretin/VIP family of peptides, is substantially structured in water
    • Blankenfeldt, W., K. Nokihara, S. Naruse, U. Lessel, D. Schomburg & V. Wray. 1996. NMR spectroscopic evidence that helodermin, unlike other members of the secretin/VIP family of peptides, is substantially structured in water. Biochemistry 35: 5955-5962.
    • (1996) Biochemistry , vol.35 , pp. 5955-5962
    • Blankenfeldt, W.1    Nokihara, K.2    Naruse, S.3    Lessel, U.4    Schomburg, D.5    Wray, V.6
  • 15
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    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
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    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 16
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    • (1980) FEBS Lett. , vol.119 , pp. 265-270
    • Wagman, M.E.1    Dobson, C.M.2    Karplus, M.3
  • 17
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    • Bodanszky, A., M. A. Ondetti, V. Mutt & M. Bodanszky. 1969. Synthesis of secretin. IV. Secondary structure in a miniature protein. J. Amer. Chem. Soc. 91: 944-949.
    • (1969) J. Amer. Chem. Soc. , vol.91 , pp. 944-949
    • Bodanszky, A.1    Ondetti, M.A.2    Mutt, V.3    Bodanszky, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.