The Library
Spatial structure of heptapeptide Glu-Ile-Leu-Asn-His-Met-Lys, a fragment of the HIV enhancer prostatic acid phosphatase, in aqueous and SDS micelle solutions
Tools
Bloсhin, Dmitri S., Aganova, Oksana V., Yulmetov, Aidar R., Filippov, Andrei V., Gizatullin, Bulat I., Afonin, Sergii, Antzutkin, Oleg N. and Klochkov, Vladimir V. (2013) Spatial structure of heptapeptide Glu-Ile-Leu-Asn-His-Met-Lys, a fragment of the HIV enhancer prostatic acid phosphatase, in aqueous and SDS micelle solutions. Journal of Molecular Structure, Volume 1033 . pp. 59-66. doi:10.1016/j.molstruc.2012.08.018 ISSN 0022-2860.
Research output not available from this repository.
Request-a-Copy directly from author or use local Library Get it For Me service.
Official URL: http://dx.doi.org/10.1016/j.molstruc.2012.08.018
Abstract
Prostatic acid phosphatase (PAP) is a protein abundantly present in human seminal fluid. PAP plays important role in fertilization. Its 39-amino-acid fragment, PAP(248–286), is effective in enhancing infectivity of HIV virus. In this work, we determined the spatial structure in aqueous solution of a heptapeptide within the PAP fragment, containing amino acid residues 266–272 (Glu-Ile-Leu-Asn-His-Met-Lys). We also report the structure of the complex formed by this heptapeptide with sodium dodecyl sulfate micelles, a model of a biological membrane, as determined by 1H NMR spectroscopy and 2D NMR (TOCSY, HSQC-HECADE, NOESY) spectroscopy. Complex formation was confirmed by chemical shift alterations in the 1H NMR spectra of the heptapeptide, as well as by the signs and values of NOE effects. We also present a comparison of the spatial structure of Glu-Ile-Leu-Asn-His-Met-Lys in water and in complex with sodium dodecyl sulfate.
Item Type: | Journal Article | ||||
---|---|---|---|---|---|
Divisions: | Faculty of Science, Engineering and Medicine > Science > Physics | ||||
Journal or Publication Title: | Journal of Molecular Structure | ||||
Publisher: | Elsevier BV | ||||
ISSN: | 0022-2860 | ||||
Official Date: | 2013 | ||||
Dates: |
|
||||
Volume: | Volume 1033 | ||||
Page Range: | pp. 59-66 | ||||
DOI: | 10.1016/j.molstruc.2012.08.018 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
Request changes or add full text files to a record
Repository staff actions (login required)
View Item |