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...

Full description

Saved in:

Bibliographic Details
Published in:	Biochemistry (Easton) Vol. 38; no. 31; p. 9850
Main Authors:	Zídek, L, Stone, M J, Lato, S M, Pagel, M D, Miao, Z, Ellington, A D, Novotny, M V
Format:	Journal Article
Language:	English
Published:	United States 03.08.1999
Subjects:	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
Online Access:	Get more information
Tags:	Add Tag No Tags, Be the first to tag this record!

Be the first to leave a comment!