Recombinant production and structural studies of the Aplysia water-borne protein pheromone enticin indicates it has a novel disulfide stabilized fold

Peptides

Volumn 28, Issue 1, 2007, Pages 94-102

  Cummins, Scott F ^a   Xie, Fang ^b   Misra, Milind ^a   Amare, Andinet ^b   Jakubowski, Jennifer A ^b   de Vries, Melissa R ^a   Sweedler, Jonathan V ^b   Nagle, Gregg T ^a   Schein, Catherine H ^a  

^a University of Texas Medical Branch School of Medicine   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

Aplysia; Attractin; Enticin; pCold III; Pheromone; Temptin

Indexed keywords

ARGININE; ATTRACTIN; COLD SHOCK PROTEIN; COMPLEMENTARY DNA; CYSTEINE; DISULFIDE; ENTICIN; GLUTAMIC ACID; PHEROMONE; PROTEINASE; RECOMBINANT PROTEIN; WATER;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; APLYSIA; APLYSIA BRASILIANA; ARTICLE; BASE PAIRING; CIRCULAR DICHROISM; DISULFIDE BOND; EGG LAYING; ENHANCER REGION; ESCHERICHIA COLI; GENE VECTOR; GENETIC CONSERVATION; IMMUNOBLOTTING; IN VIVO STUDY; MASS SPECTROMETRY; MATING; MOLECULAR CLONING; MOLECULAR RECOGNITION; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN ISOLATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN SECRETION; PROTEIN STABILITY; PROTEIN STRUCTURE; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; WESTERN BLOTTING;

AMINO ACID SEQUENCE; ANIMALS; APLYSIA; BLOTTING, WESTERN; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; DISULFIDES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; MODELS, GENETIC; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHEROMONES; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

APLYSIA; APLYSIA BRASILIANA; APLYSIA CALIFORNICA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 33845600781     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2006.08.027     Document Type: Article

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