Structure of antimicrobial peptide anoplin in DPC micelles
dodecyl 2-(trimethylammonio)ethyl phosphate
Rational Design of Alpha-Helical Antimicrobial Peptides: Do's and Don'ts.
pseudo-3D-inversion recovery weighted NOESY
DODECYL 2-(TRIMETHYLAMMONIO)ETHYL PHOSPHATE-2
DODECYL 2-(TRIMETHYLAMMONIO)ETHYL PHOSPHATE-6
THE ORIENTATION OF THE PEPTIDE WITHIN THE MICELLE WAS DETERMINED FROM EXPERIMENTAL DATA (PARAMAGNETIC RELAXATION ENHANCEMENTS). THE RESTRAINT FILE CONTAINS DISTANCE RESTRAINTS FROM PEPTIDE ATOMS TO THE MICELLE CENTER, WHICH IS REPRESENTED AS THE PSEUDOATOM X, RESIDUE UNX. FIRST STEP: IN VACUO WITH NOVA FORCE FIELD. SECOND STEP: IN EXPLICIT SOLVENT (WATER/MICELLE) WITH YASARA FORCE FIELD.
3 mM anoplin, 150 mM [U-98% 2H] DODECYL 2-(TRIMETHYLAMMONIO)ETHYL PHOSPHATE, 10 mM potassium phosphate, 2 mM sodium azide, 95% H2O/5% D2O
3 mM anoplin, 150 mM [U-98% 2H] DODECYL 2-(TRIMETHYLAMMONIO)ETHYL PHOSPHATE, 10 mM potassium phosphate, 2 mM sodium azide, 0-10 mM Gd(DTPA-BMA), 95% H2O/5% D2O
amphipathic helix, ANTIMICROBIAL PROTEIN