Abstract
Protein hubs in protein–protein interaction network are especially important due to their central roles in the entire network. Despite of their importance, the folding kinetics of hub proteins in comparison with non-hubs is still unknown. In this work, the folding rates for protein hubs and non-hubs were predicted and compared for the interactome of Escherichia coli K12, and the results showed that hub proteins fold faster than non-hub proteins. A possible explanation might be that protein hubs have more and fast-folding structural conformations than non-hubs, which leads to the notion of “hub of hubs” in the protein conformation space. It was found that the sequence and structure features relevant to protein folding rates are also different between hub and non-hub proteins. Moreover, the interacting proteins tend to have similar folding rates. These results gave insightful implications for understanding the interplay between the mechanisms of protein folding and interaction.
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Acknowledgments
We’d like to thank Bao-Hai Hao for his assistance in data analysis and helpful discussion. This work was supported by the National Natural Science Foundation of China (31570844, 31100602), the National Basic Research Program of China (973 project, Grant 2013CB127103), Project J1103510 supported by NSFC, Project 2010QC016, 2011PY070 and 2013JC009 supported by the Fundamental Research Funds for the Central Universities, and the Scientific Research Foundation for the Returned Overseas Chinese Scholars, State Education Ministry of China. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
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Xu, HR., Cheng, JF., Hu, XP. et al. Are protein hubs faster folders? Exploration based on Escherichia coli proteome. Amino Acids 48, 2747–2753 (2016). https://doi.org/10.1007/s00726-016-2309-x
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DOI: https://doi.org/10.1007/s00726-016-2309-x