It seems an important question to me. D-, L-aspartic acid can be separated by Avidin-affinity-HPLC column, but separation becomes weaker using organic modifier (please see file; D-Asp Avidin 1). I have determined D,L-α-lipoic acid ((±)- thioctic acid) since D- and L- α-lipoic acid can not be separated by my hand (please see file; Thioctic acid Determination). I have now considering that sulphur atom gives some degrees of hydrophobicity to the sulphur-containing molecules.
Thank you very much for your kind indication. I have used the hydrophobicity of University of Wisconsin, Madison, WI, USA, but not satisfying to me with respect to Keratin-associated proteins (please see file; Hydrophobicity Capaldi).
Therefore, I can improve the calculation method at this time considering the hydrophobicity of sulphur atoms; i.e.,
old hydrophobicity 0.594 improved hydrophobicity 0.765
Keratin-associated protein 5-5
old hydrophobicity 0.713 improved hydrophobicity 0.777
Keratin-associated protein 4-1
old hydrophobicity 0.575 improved hydrophobicity 0.721
This new result matches well with our recent result for KAP (please see file; JMBT Alopecia).
This new calculation method is powerful to sulphate-rich membrane proteins and hormones.
Insulin
A chain: GIVEQCCTSICSLYQLENYCN
B chain: FVNQHLCGSHLVEALYLVCGERGFFYTPKT
old hydrophobicity 0.607 improved hydrophobicity 0.641
Insulin receptor (INSR)
old hydrophobicity 0.533 improved hydrophobicity 0.539
Growth hormone (Somatotropin)
old hydrophobicity 0.487 improved hydrophobicity 0.493
Growth hormone receptor
old hydrophobicity 0.499 improved hydrophobicity 0.505
Thank you again to Dr. Murwan khalid Sabahelkhier (Faculty of Science and Technology, Al-Neelain University, Khartoum, Sudan) to leading me to this important conclusion.