Sakacin P variant that is structurally stabilized by an inserted C-terminal disulfide bridge.
Three-Dimensional Structure in Lipid Micelles of the Pediocin-Like Antimicrobial Peptide Sakacin P and a Sakacin P Variant that is Structurally Stabilized by an Inserted C-Terminal Disulfide Bridge
THREE-DIMENSIONAL STRUCTURE IN LIPID MICELLES OF THE PEDIOCIN-LIKE ANTIMICROBIAL PEPTIDE SAKACIN P.
ENGINEERED MUTATION IN CHAIN A: CYS 42 TO ASN 42 SAKACIN P VARIANT THAT IS STRUCTURALLY STABILIZED BY AN INSERTED C-TERMINAL DISULFIDE BRIDGE.
THE SEQUENCE IS DESCRIBED IN J. BACTERIOL. 182, 2643-2648
THE STRUCTURES WERE DETERMINED USING A COMBINATION OF 1H NMR SPECTROSCOPIC METHODS FOLLOWED BY DISTANCE GEOMETRY/SIMULATED ANNEALING CALCULATIONS.
LEAST RESTRAIN VIOLATION AND OVERALL ENERGY
AMBER 6, SAN FRANCISCO, UNIVERSITY OF CALIFORNIA, 1999.
250 MM DPC/10% D2O/ 0.1% TFA/1MM PEPTIDE
CASE, D.A., PEARLMAN, D.A., CALDWELL, III, J.C., ET AL.
ANTIBIOTIC, PEDIOCIN-LIKE BACTERIOCINS, ANTIMICROBIAL PEPTIDES, SAKACIN ANTIBIOTIC, BACTERIOCIN