Revealing the membrane-bound structure of neurokinin A using neutron diffraction

Malcolm J.M. Darkes, Thomas Hauss, Silvia Dante, Jeremy P. Bradshaw

Research output: Contribution to journalConference article

3 Citations (Scopus)

Abstract

Neurokinin A (or substance K) belongs to the tachykinin family, a group of small amphipathic peptides that bind to specific membrane-embedded, G-protein coupled receptors. The agonist/receptor complex is quaternary in nature because the receptor binding sites are thought to be located within the lipid bilayer and because the role of water cannot be ignored. The cell membrane acts as a solvent to accumulate peptide and an inducer of peptide secondary structure. The three-dimensional shape that the peptide assumes when associated to the cell membrane will be an important parameter with regards to the receptor selectivity and affinity. Neutron diffraction measurements were carried out in order to define the location of the N-terminus of the peptide in synthetic phospholipid multi-bilayer stacks.

Original languageEnglish
Pages (from-to)505-507
Number of pages3
JournalPhysica B: Condensed Matter
Volume276-278
DOIs
Publication statusPublished - 1 Mar 2000
Event2nd European Conference on Neutron Scattering (ECNS '99) - Budapest, Hung
Duration: 1 Sep 19994 Sep 1999

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Condensed Matter Physics
  • Electrical and Electronic Engineering

Cite this

Revealing the membrane-bound structure of neurokinin A using neutron diffraction. / Darkes, Malcolm J.M.; Hauss, Thomas; Dante, Silvia; Bradshaw, Jeremy P.

In: Physica B: Condensed Matter, Vol. 276-278, 01.03.2000, p. 505-507.

Research output: Contribution to journalConference article

Darkes, Malcolm J.M. ; Hauss, Thomas ; Dante, Silvia ; Bradshaw, Jeremy P. / Revealing the membrane-bound structure of neurokinin A using neutron diffraction. In: Physica B: Condensed Matter. 2000 ; Vol. 276-278. pp. 505-507.
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