A 24-residue peptide called Pandinin 2, isolated from scorpion venom, was found to have both antimicrobial and hemolytic properties. The sequence of the first 18 residues of this peptide is shown below. The peptide forms a helix in which nonpolar amino acids are on one side of helix and polar or charged amino acids are on the other side of the helix. FWGALAKGALKLIPSLFS Examine the 18 residue sequence for Pandinin 2 and predict which amino acid side chains are likely to be found on the nonpolar side of the amphipathic helix. List the residues from left to right using one-letter abbreviations. Use single-letter abbreviations with no spaces.

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Chapter1: Biochemistry: An Evolving Science
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A 24-residue peptide called Pandinin 2. isolated from scorpion venom, was found to have both antimicrobial and hemolytic properties.
The sequence of the first 18 residues of this peptide is shown below. The peptide forms a helix in which nonpolar amino acids are on
one side of helix and polar or charged amino acids are on the other side of the helix.
FWGALAKGALKLIPSLFS
Examine the 18 residue sequence for Pandinin 2 and predict which amino acid side chains are likely to be found on the nonpolar
side of the amphipathic helix. List the residues from left to right using one-letter abbreviations. Use single-letter abbreviations
with no spaces.
eTextbook and Media
Pandinin 2 is able to lyse bacteria and red blood cells; this is because the hydrophilic side of the helix interacts favorably
with the nonpolar membrane, disrupting its structure and killing the cell.
Transcribed Image Text:Current Attempt in Progress A 24-residue peptide called Pandinin 2. isolated from scorpion venom, was found to have both antimicrobial and hemolytic properties. The sequence of the first 18 residues of this peptide is shown below. The peptide forms a helix in which nonpolar amino acids are on one side of helix and polar or charged amino acids are on the other side of the helix. FWGALAKGALKLIPSLFS Examine the 18 residue sequence for Pandinin 2 and predict which amino acid side chains are likely to be found on the nonpolar side of the amphipathic helix. List the residues from left to right using one-letter abbreviations. Use single-letter abbreviations with no spaces. eTextbook and Media Pandinin 2 is able to lyse bacteria and red blood cells; this is because the hydrophilic side of the helix interacts favorably with the nonpolar membrane, disrupting its structure and killing the cell.
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