Hydrophobic packing and spatial arrangement of amino acid residues in globular proteins.
Amino acid residues acquire characteristic hydrophobic environments in globular proteins. Using the crystal data on 21 proteins, a new scale of hydrophobic indices for the residues is set up. This scale provides valuable information with regard to hydrophobic domains, nucleation sites, surface domains, loop sites and the spatial positions of residues in protein molecules.
D000596:Amino Acids / Q000032:analysis*; D003460:Crystallization; D005916:Globulins; D008433:Mathematics; D011487:Protein Conformation; D014867:Water; D014961:X-Ray Diffraction
D000596:Amino Acids; D005916:Globulins; D014867:Water