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We followed the aggregate size distribution evolving during the series of eight independent trajectories per peptide system.
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Peptides were synthesized by solid-phase multiple peptide system (Houghten 1985; Jeener et al. 1979).
All peptides were prepared under conditions of Good Manufacturing Practice using a Multiple Peptide System (San Diego, CA).
The patterns of peptide strand registry were found to be heterogeneous in both peptide systems.
Histological differences were also noted between the two peptide systems.
During the simulations the three-peptide system explores several configurations.
The mature peptides of several two-peptide systems share structural and sequence homology with known single-peptide lantibiotics.
In contrast, L. reuteri strain only has one functional peptide transport system, the DtpT system.
The MRM method included 280 transitions from 33 proteins (2 3 peptides per protein, 3 4 transitions per peptide; Table 2; Additional file 1).
Following the PlasmaDeepDive™ protocol, three transitions per peptide were used for detection.
Isothermal titration calorimetry and mass spectrometry indicate a binding stoichiometry of at least three metals bound per peptide strand.
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