Glutamic acid relative hydrophobicity

Positive ROA bands in the range 1297-1312 cm-1 are also characteristic of a-helix. These are observed at 1300 cm-1 in human serum albumin (Fig. 4) and at 1297 cm-1 in a-helical poly-L-lysine (Fig. 3). These additional bands appear to be associated with a-helix in a more hydrophobic environment (Barron etal., 2000). The striking absence of a positive ROA band in the range 1297-1312 cm-1 in a-helical poly-L-glutamic acid would then suggest that only the hydrated form of a-helix is present, possibly due to the shorter side chains relative to poly-L-lysine,... 

The thermodynamic stability, the aggregation state, and the relative orientation of the helical strands in such peptides were shown to depend largely on the identity of the amino acid residues at positions a, d, e, and g. The use of leucine and valine at the hydrophobic core (positions a and glutamic acid and lysine at the e and g positions were shown to control equilibrium between dimeric and trimeric coiled-coil aggregation states." Peptide sequences that allow interconversion between dimeric and trimeric parallel coiled coils were found as productive templates to enhance substrate selectivity, catalytic efficiency, and turnover and were commonly used in peptide-replicating systems. 

For assembly of novel three-dimensional (3D) structures, block copolypeptides are required that have structural domains (i.e., amino acid sequences) whose size and composition can be precisely adjusted. Such materials have proven elusive using conventional techniques. Strong base-initiated NCA polymerizations are very fast. These polymerizations are poorly understood and well-defined block copolymers cannot be prepared. Primary amine-initiated NCA polymerizations are also not free of side reactions. Even after fractionation of the crude preparations, the resulting polypeptides are relatively ill-defined, which may complicate unequivocal evaluation of their properties and potential applications. Nevertheless, there are many reports on the preparation of block copolypeptides using conventional primary amine initiators. Examples include many hydrophilic-hydrophobic and hydrophilic-hydrophobic-hydrophilic di- and triblock copolypeptides (where hydrophilic residues were glutamate and lysine, and hydrophobic residues were leucine, valine, isoleucine, phenylalanine, and alanine" ) prepared to study... 

---