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Contact and association of hydrophilic peptides and peripheral proteins with
cellular membranes are commonly found through the sequence motifs which
contain basic and aromatic amino acid residues. Those sequence motifs are not
only critical for protein binding but also important for local disruption and penetra-
tion of membranes, for recruitment of lipids, and for membrane fusion [ 159 - 165 ].
However, the locations and insertion depths in membrane lipids are quite different
as compared with those residues in for transmembrane proteins. It is not straight-
forward to apply those well established principles generalized from transmem-
brane proteins to peripheral membrane proteins. For example, we have recently
investigated the insertion depth of Trp residue into POPC lipid bilayers in
different peptide sequencing, as shown in Fig. 10 . Clearly the penetration depth
of the side chain of Try residue in AWA and VAMP2 peptides are deeper than the
1
Fig. 10
H MAS NOESY spectra of indole ( black ), AWA ( red ), and VAMP2 ( blue ). The indole
structure and numbering are for aid of peak assignment
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