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  Conformation of [8‐arginine]vasopressin and V1 antagonists in dimethyl sulfoxide solution derived from two‐dimensional NMR spectroscopy and molecular dynamics simulation

Schmidt, J. M., Ohlenschläger, O., Rüterjans, H., Grzonka, Z., Kojro, E., Pávó, I., et al. (1991). Conformation of [8‐arginine]vasopressin and V1 antagonists in dimethyl sulfoxide solution derived from two‐dimensional NMR spectroscopy and molecular dynamics simulation. European Journal of Biochemistry, 201(2), 355-371. doi:10.1111/j.1432-1033.1991.tb16293.x.

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 Creators:
Schmidt, Jürgen M.1, Author
Ohlenschläger, Oliver1, Author
Rüterjans, Heinz1, Author
Grzonka, Zbigniew2, Author
Kojro, Elzbieta3, Author           
Pávó, Imre3, Author           
Fahrenholz, Falk3, Author           
Affiliations:
1Institut für Biophysikalische Chemie, Johann Wolfgang Goethe‐Universität Frankfurt, Frankfurt am Main, Federal Republic of Germany, ou_persistent22              
2Institute of Chemistry, University of Gdansk, Poland, ou_persistent22              
3Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_3273414              

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 Abstract: Structural and dynamic properties of [8‐arginine]vasopressin and a class of highly potent vasopressin V1 antagonists which contain 3‐mercepto‐3, 3‐cyclopentamethylene propionic acid (Mca) in position 1 of the vasopressin sequence have been determined. On the basis of two‐dimensional NMR experiments in dimethyl sulfoxide solution, interproton distances were derived according to which model conformations were built and refined using molecular dynamics simulations. The antagonistic property was found to be related to an inversed chirality of the disulfide bridge. In all investigated molecules, characteristic β‐turn structure elements were found for the backbone conformation of the endocyclic residues Tyr2–Asn5. For this portion of the peptide sequence, various conformational equilibria were detected which matched different time scales. For [Arg8]vasopressin, averaged NMR parameters were obtained which could be explained by rapid interconversion between different β‐turn geometries, whereas multiple slowly exchanging conformations were observed for the V1 antagonists. V1 antagonists containing sarcosine in position 7 exhibited multiple spectral patterns for the exocyclic part attributed tocis/trans isomerization. The X‐ray structure of deamino‐oxytocin [Wood, S. P., Tickle, I. J., Treharne, A. M., Pitts, J. E., Mascarenhas, Y., Li, J. Y., Husain, J., Cooper, S., Blundell, T. L., Hruby, V. J., Buku, A., Fischman, A. J. & Wyssbrod, H. R. (1986) Science 232, 633–636] was found to represent one sample of the conformational space covered by the multiple conformations found for [Mca1, Arg8]vasopressin.

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Language(s): eng - English
 Dates: 1991-06-031991-02-132005-03-031991-10-01
 Publication Status: Published in print
 Pages: 17
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 201 (2) Sequence Number: - Start / End Page: 355 - 371 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040