Structure of D19S variant of the Penicillium Antifungal Protein (PAF)
D19S Mutation of the Cationic, Cysteine-Rich Protein PAF: Novel Insights into Its Structural Dynamics, Thermal Unfolding and Antifungal Function.
This variant of Penicillium Antifungal Protein (PAF) is produced by a aspartic acid to serine mutation of residue 19. By this single residue exchange the antifungal function of the protein has been dramatically modified.
Structure of Penicillium antifungal protein (PAF) with the native sequence
Chemical shift list of 15N-13C labelled PAF with the native sequence
simulated annealing, torsion angle dynamics
1.7 mM [U-100% 15N] PAFD19S, 5 v/v [U-2H] D2O, 40 mM sodium chloride, 10 mM sodium phosphate, 0.04 % potassium phosphate, 95% H2O/5% D2O