| Popis: |
By using one Asp or one Glu per thirty residues in a polytricosapeptide capable of exhibiting a hydrophobic folding and assembly transition and stepwise converting a set of the five Val residues (most proximal to the Asp or Glu residue) to more-hydrophobic Phe residues, a non-linear hydrophobic-induced p K a shift was observed with a Δ p K a of 0.4 (Asp) and 0.3 (Glu) on addition to 2 Phe residues per 30mer but with a Δ p K a of 4.7 (Asp) and 2.7 (Glu) on going from 4 Phe/30mer to 5 Phe/30mer. As a shift in p K a can be equivalent to the conversion to chemical energy from whatever energy input — mechanical, chemical, electrochemical, pressure or light — which effects a change in hydrophobicity, the non-linear hydrophobic-induced p K a shift means increased efficiency of energy conversion with increased hydrophobicity of the protein-based polymer. |
Full Text from ScienceDirect