Selvaraj S, Gromiha M M
Department of Physics, Bharathidasan University, Tamil Nadu, India.
J Protein Chem. 1998 Oct;17(7):691-7. doi: 10.1007/BF02780972.
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.
蛋白质结构通过局部和远程相互作用得以稳定。在这项工作中，我们从残基距离的角度分析了远程相互作用在（α/β）8桶状蛋白质中的重要性。我们发现，相隔21 - 30个残基范围内出现的残基对远程接触的贡献更大。实际上，在这些蛋白质中，约50%的连续链段出现在21 - 30个残基的序列距离处。芳香族氨基酸残基苯丙氨酸（Phe）、色氨酸（Trp）和酪氨酸（Tyr）倾向于4 - 10的范围，而所有其他残基则倾向于21 - 30的范围。疏水 - 疏水残基对是远程相互作用中最优先的，它们可能在（α/β）8桶状蛋白质的折叠和稳定中起关键作用。
