title: 1H, 15N and 13C resonance assignment of darcin, a mouse major urinary protein.
abstract: Darcin is an important lipocalin of the urinary MUP family. These beta-barrel structures differ subtly in sequence and function and facilitate communication between members of the mouse population via scent marks. Polymorphism within the family has led to the hypothesis that individual MUPs can also contribute to social and physiological information of the scent owner and thus demonstrates the necessity for structural investigation of these variations. Using conventional triple resonance experiments, (1)H (15)N and (13)C assignment of recombinant N terminal hexa-histidine tagged Darcin has been achieved. The corresponding chemical shifts have been deposited in the BioMagResBank; Accession No. 16840.
authors: NMR Centre for Structural Biology, Biological Sciences, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK.
authors: Marie M
authors: MM
authors: Phelan
authors: Lynn
authors: L
authors: McLean
authors: Deborah M
authors: DM
authors: Simpson
authors: Jane L
authors: JL
authors: Hurst
authors: Robert J
authors: RJ
authors: Beynon
authors: Lu-Yun
authors: LY
authors: Lian
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002247:Carbon Isotopes; D006859:Hydrogen; D036341:Intercellular Signaling Peptides and Proteins; D051379:Mice; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D011506:Proteins / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D002247:Carbon Isotopes; D036341:Intercellular Signaling Peptides and Proteins; C555029:Mup20 protein, mouse; D009587:Nitrogen Isotopes; D011506:Proteins; D011994:Recombinant Proteins; C035737:major urinary proteins; D006859:Hydrogen