Importance of the single amino acid potential in water for secondary and tertiary structures of proteins

The reliable single amino acid potential (SAAP) functions are obtained for glycine and alanine in water and ether by applying the self-consistent isodensity polarizable continuum model (SPIPCM) method. The results have shown that the intrinsic conformational preferences of the individual amino acids in water are of significant importance not only for describing conformations of a polypeptide chain in the random coil but also for understanding the folding to the secondary and tertiary structures.