Conformations of cysteine disulfides were analyzed in X-ray, nuclear magnetic resonance (NMR), and co-crystal structures of peptide toxins retrieved from Protein Data Bank. The parameters side chain t
(A) Serial 5-fold dilutions of exponentially growing S. cerevisiae BY4741 cells treated with 64 µM of each peptide for 24 h, and subsequently plated onto YPD peptide-free plates. (B) Brightfield (imag
