Figure 4.

The p-values for secondary structure and relative surface accessibility preferences for the statistically significant amino acids in thermophilic proteins among the three folds. The eight state classification of DSSP was reduced into three states (Helix, Sheet, and Loop) as described in the text. The amino acids are classified into three classes according to relative surface accessibility: buried, if less than 9%; intermediate, if between 9-36%; and exposed, if more than 36% [43]. The statistically significant secondary structure and solvent exposure preferences for amino acids are bolded and underlined and p-values are provided. Our analysis showed that the significant amino acids in mesophilic proteins do not show statistically significant preferences for secondary structure or solvent exposure.

Yennamalli et al. BMC Structural Biology 2011 11:10   doi:10.1186/1472-6807-11-10
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