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 language | English |
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Pages (from-to) | 505-507 |
Number of pages | 3 |
Journal | Physica B: Condensed Matter |
Volume | 276-278 |
DOIs | |
Publication status | Published - 1 Mar 2000 |
Event | 2nd European Conference on Neutron Scattering (ECNS '99) - Budapest, Hung Duration: 1 Sep 1999 → 4 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 journal › Conference article
}
TY - JOUR
T1 - Revealing the membrane-bound structure of neurokinin A using neutron diffraction
AU - Darkes, Malcolm J.M.
AU - Hauss, Thomas
AU - Dante, Silvia
AU - Bradshaw, Jeremy P.
PY - 2000/3/1
Y1 - 2000/3/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0033876391&partnerID=8YFLogxK
U2 - 10.1016/S0921-4526(99)01353-8
DO - 10.1016/S0921-4526(99)01353-8
M3 - Conference article
VL - 276-278
SP - 505
EP - 507
JO - Physica B: Condensed Matter
JF - Physica B: Condensed Matter
SN - 0921-4526
ER -