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Effect of disulfide bridges deletion on the conformation of the androctonin, polyphemusin I, and thanatin antimicrobial peptides: molecular dynamics simulation studies

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Figure

Table 1. Primary structures of the wild peptides and their re- spective mutants. The residues where the mutation was made are in bold letter
Table 5. Hydrogen bonds found in the thanatin and thany2 simulations.
Table 6. The maxima of the Ramachandran angles distribu- tions for the androctonin and andry4 peptides
Table 7. The maxima of the Ramachandran angles distribu- tions for the polyphemusin-I and poly4 peptides
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