The role of local tight packing of hydrophobic groups in beta-structure.
An analysis of the tendency of hydrophobic groups to tight packing on the surface of beta-sheets based on well-known parameters of beta-sheets and hydrophobic groups was conducted. This analysis shows the existence of very limited numbers and clearly outlined architecture families of regular parts for the majority of beta-structure-containing domains. Each family of architecture strongly depends on the number of beta-strands in the pure beta-domains and on the existence and number of additional alpha-helixes and on the mutual arrangements beta-strands and alpha-helixes along the chain in mixed alpha/beta-domains. This paper demonstrates that the tendency of hydrophobic groups to the local tight packing on the surface of beta-sheets is probably the main reason for the twist of beta-sheets.
Vtyurin
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Department of Biopolymers Structure and Functional Research, Russian Academy of Sciences, Moscow.
D000595:Amino Acid Sequence; D004798:Enzymes / Q000737:chemistry*; D005418:Flavodoxin / Q000737:chemistry; D006860:Hydrogen Bonding; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D012995:Solubility; D012997:Solvents; D014305:Triose-Phosphate Isomerase / Q000737:chemistry; D014357:Trypsin / Q000737:chemistry
D004798:Enzymes; D005418:Flavodoxin; D010446:Peptide Fragments; D011506:Proteins; D012997:Solvents; D014357:Trypsin; D014305:Triose-Phosphate Isomerase