title: Importance of long-range interactions in (alpha/beta)8 barrel fold.
abstract: Protein structures are stabilized by both local and long-range interactions. In this work, we analyzed the importance of long-range interactions in (alpha/beta)8 barrel proteins in terms of residue distances. We found that the residues occurring in the range of 21-30 residues apart contribute more toward long-range contacts. Indeed, about 50% of successive strands in these proteins are found to occur at a sequential distance of 21-30 residues. The aromatic amino acid residues Phe, Trp, and Tyr prefer the 4-10 range and all other residues prefer the 21-30 range. Hydrophobic-hydrophobic residue pairs are the most preferred ones for long-range interactions and they may play a key role in the folding and stabilization of (alpha/beta)8 barrel proteins.
authors.affiliation: Department of Physics, Bharathidasan University, Tamil Nadu, India.
authors.forename: S
authors.initials: S
authors.lastname: Selvaraj
authors.forename: M M
authors.initials: MM
authors.lastname: Gromiha
mesh_terms: D000596:Amino Acids / Q000032:analysis; D018360:Crystallography, X-Ray; D016208:Databases, Factual; D008956:Models, Chemical; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D000596:Amino Acids