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 to be exposed or buried; mean force potentials that characterize the residues' free energy dependence on their degree of exposure; the average composition of water soluble proteins, and the composition of their core and surface. The nature of differences between different hydrophobicity-related scales is discussed.
Nauchitel
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Oklahoma University Health Sciences Center, Oklahoma City 73190.
Somorjai
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D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D008956:Models, Chemical; D008969:Molecular Sequence Data; D009211:Myoglobin / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D012995:Solubility; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
D000596:Amino Acids; D009211:Myoglobin; D010940:Plant Proteins; D011506:Proteins; D014867:Water; C024934:crambin protein, Crambe abyssinica