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Solution conformations of an insect neuropeptide: crustacean cardioactive peptide (CCAP)
Dept. Chemistry, Cape Town, South Africa.
Dept. Chemistry, Cape Town, South Africa.
Dept. Chemistry, Cape Town, South Africa.
Dept. Chemistry, Cape Town, South Africa.
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2009 (English)In: Peptides, ISSN 0196-9781, E-ISSN 1873-5169, Vol. 30, no 3, 557-564 p.Article in journal (Refereed) Published
Abstract [en]

The solution structure of crustacean cardioactive peptide (CCAP), a cyclic amidated nonapeptide neurohormone, was studied using molecular dynamics techniques, with constraints derived from NMR studies in water and water/dodecylphosphocholine micellar medium. This peptide, found in various invertebrates, has the primary sequence Pro(1) Phe(2) Cys(3) Asn(4) Ala(5) Phe(6) Thr(7) Gly(8) Cys(9) NH(2), with an intramolecular disulfide bridge between the two cysteine residues. In aqueous solution the peptide was found to have a type(IV) beta-turn between residues 5-8. In a water/decane biphasic medium a type(IV) beta-turn between residues 3 and 6 and two classic gamma-turns between residues 4-6 and 7-9, were found. Analysis of the (1)H and (13)C NMR chemical shifts data showed that the model free S(2) order parameter of the residues varied between 0.65 and 0.9. The molecular dynamic root mean square fluctuations of structural ensembles of the backbone varied between 0.5 and 2.2 with the central residues showing the least fluctuations.

Place, publisher, year, edition, pages
2009. Vol. 30, no 3, 557-564 p.
Keyword [en]
CCAP, Arthropod neuropeptide, GROMACS, Molecular dynamics, Dodecylphosphocholine
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:uu:diva-104077DOI: 10.1016/j.peptides.2008.11.014ISI: 000264791300015PubMedID: 19103242OAI: oai:DiVA.org:uu-104077DiVA: diva2:219350
Available from: 2009-05-27 Created: 2009-05-27 Last updated: 2017-12-13Bibliographically approved

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