NMR mapping of the recombinant mouse major urinary protein I binding site occupied by the pheromone 2-sec-butyl-4,5-dihydrothiazole

The interactions between the mouse major urinary protein isoform MUP-I and the pheromone 2-sec-butyl-4,5-dihydrothiazole have been characterized in solution. (15)N-labeled and (15)N, (13)C-doubly-labeled recombinant MUP-I were produced in a bacterial expression system and purified to homogeneity. Ra...

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Vydáno v:	Biochemistry (Easton) Ročník 38; číslo 31; s. 9850
Hlavní autoři:	Zídek, L, Stone, M J, Lato, S M, Pagel, M D, Miao, Z, Ellington, A D, Novotny, M V
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States 03.08.1999
Témata:	Amino Acid Sequence Animals Binding Sites Carbon Isotopes Escherichia coli - genetics Macromolecular Substances Mice Molecular Sequence Data Nitrogen Isotopes Nuclear Magnetic Resonance, Biomolecular - methods Peptide Mapping - methods Pheromones - chemistry Pheromones - metabolism Protein Isoforms - chemistry Protein Isoforms - genetics Protein Isoforms - metabolism Protein Structure, Secondary Proteins - chemistry Proteins - genetics Proteins - metabolism Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - metabolism Thiazoles - chemistry Thiazoles - metabolism
ISSN:	0006-2960
On-line přístup:	Zjistit podrobnosti o přístupu
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