Predicting protein folding cores by empirical potential functions |
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Authors: | Mingzhi Chen Athanasios D Dousis Yinghao Wu Jianpeng Ma |
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Institution: | a Graduate Program of Structural and Computational Biology and Molecular Biophysics, USA b Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, BCM-125, Houston, TX 77030, USA c Department of Bioengineering, Rice University, 6100 Main Street, Houston, TX 77005, USA d Chemistry Department, Umeå University, SE-901 87 Umeå, Sweden |
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Abstract: | Theoretical and in vitro experiments suggest that protein folding cores form early in the process of folding, and that proteins may have evolved to optimize both folding speed and native-state stability. In our previous work (Chen et al., Structure, 14 (2006) 1401), we developed a set of empirical potential functions and used them to analyze interaction energies among secondary-structure elements in two β-sandwich proteins. Our work on this group of proteins demonstrated that the predicted folding core also harbors residues that form native-like interactions early in the folding reaction. In the current work, we have tested our empirical potential functions on structurally-different proteins for which the folding cores have been revealed by protein hydrogen-deuterium exchange experiments. Using a set of 29 unrelated proteins, which have been extensively studied in the literature, we demonstrate that the average prediction result from our method is significantly better than predictions based on other computational methods. Our study is an important step towards the ultimate goal of understanding the correlation between folding cores and native structures. |
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Keywords: | Protein folding Folding cores Folding nuclei HX Hydrogen exchange phi-value |
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