22.4 Experimental Measures and Modeling Techniques
..................
~ 529
22.3
.. .... \ .... . .j
FIGURE
Side view of an amphiphilic and laterally amphipathic peptide, with one face of
the helix displaying hydrophobic residues, and the opposite face displaying hy-
drophilic residues.
hydrophilic amino acids (Figure 22.4). A number of polar, acidic, or basic amino
acids are required within the peptide to impart suitable solubility characteristics
(Fasman 1989).
Transmembrane pores or channels may arise from the insertion of mono-
meric peptides, where the pore is part of the secondary structure of the mono-
mer. ...
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