SPATIAL AND FREE-ENERGY DISTRIBUTION PATTERNS OF AMINO-ACID-RESIDUES IN WATER-SOLUBLE PROTEINS

We have calculated, for the 20 common amino acid residues: probability density functions that characterize the residues' tendency to occupy different locations in proteins; a propensity scale for the residues t o be exposed or buried; mean force potentials that characterize the re sidues' free energy dependence on their degree of exposure; the averag e composition of water soluble proteins, and the composition of their core and surface. The nature of differences between different hydropho bicity-related scales is discussed.