title: Aspects of the molecular structure and dynamics of neuropeptide Y.
abstract: Human neuropeptide Y (hNPY) and the Q34-->P34 mutant (P34-hNPY) have been characterized by CD spectroscopy. hNPY self-associates in aqueous solution with a dimerization constant in the micromolar range. The self-association correlates with an increase in secondary-structure content which was studied as a function of concentration, temperature and pH. The effects of temperature were measured in water (5-84 degrees C) and in ethanediol/water (2 : 1) (-90 degrees to +90 degrees C). A single-residue mutation, Q34-->P34, affects the pH, thermal and self-association properties of NPY. The CD results are correlated with photochemically induced dynamic nuclear polarization NMR experiments which show that the tyrosines at the interface between two monomer units present limited accessibility to a photoreactive dye. An equilibrium state is described, involving a PP-fold monomer form and a handshake dimer form, that accommodates the physicochemical properties of NPY.
authors: Department of Pharmacy, King's College, London, UK.
authors: A
authors: A
authors: Nordmann
authors: M J
authors: MJ
authors: Blommers
authors: H
authors: H
authors: Fretz
authors: T
authors: T
authors: Arvinte
authors: A F
authors: AF
authors: Drake
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D019281:Dimerization; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009478:Neuropeptide Y / Q000737:chemistry* / Q000235:genetics; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics; D010777:Photochemistry; D017354:Point Mutation; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013696:Temperature
chemical_list: D009478:Neuropeptide Y; D010446:Peptide Fragments