Role of hydrophobic clusters and long-range contact networks in the folding of (alpha/beta)8 barrel proteins |
| |
| Authors: | Selvaraj S Gromiha M Michael |
| |
| Affiliation: | Computational Biology Research Center (CBRC), Institute of Advanced Industrial Science and Technology (AIST) 2-41-6 Aomi, Koto-ku, Tokyo 135-0064, Japan. |
| |
| Abstract: | ![]()
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. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect PubMed 等数据库收录！ |
|
