Role of hydrophobic clusters and long-range contact networks in the folding of (α/β)8 barrel proteins
Role of hydrophobic clusters and long-range contact networks in the folding of (α/β)8 barrel proteins
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DOI：
10.1016/s0006-3495(03)75000-0
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发表时间：
2003-03-01
影响因子：
3.4
通讯作者：
Gromiha, MM
中科院分区：
文献类型：
--
作者：
Selvaraj, S;Gromiha, MM
对（α/β）（8）桶蛋白的三维结构的分析为理解负责指导和维持其共同折叠的因素提供了充足的光线。在这项工作中，在92%的所考虑的（α/β）（8）桶蛋白中鉴定出疏水富集簇。具有疏水簇的残基片段具有高的热稳定性。此外，这些簇是通过远程相互作用形成和稳定的。具体地，长程接触的网络连接（α/β）（8）桶结构域的相邻β链和疏水簇。提出了疏水簇和长程网络在为（α/β）（8）桶蛋白的折叠提供可行的共同机制方面的影响。
Analysis on the three dimensional structures of (alpha/beta)(8) barrel proteins provides ample light to understand the factors that are responsible for directing and maintaining their common fold. In this work, the hydrophobically enriched clusters are identified in 92% of the considered (alpha/beta)(8) barrel proteins. The residue segments with hydrophobic clusters have high thermal stability. Further, these clusters are formed and stabilized through long-range interactions. Specifically, a network of long-range contacts connects adjacent beta-strands of the (alpha/beta)(8) barrel domain and the hydrophobic clusters. The implications of hydrophobic clusters and long-range networks in providing a feasible common mechanism for the folding of (alpha/beta)(8) barrel proteins are proposed.