Secondary structure composition of full length HpDprA and its individual domains.

The secondary structure of individual proteins have been calculated using K2D2, a web server to estimate the α helix and β strand content of a protein from its circular dichroism spectrum and compared with the % α –helix and % β sheet calculated from HpDprA structure published by Wang et. al., (2014). RMSD values depicting goodness of fit has been shown in bracket.
Secondary structure composition of full length HpDprA and its individual domains.

已使用在线服务器K2D2计算单个蛋白质的二级结构：该服务器可通过蛋白质的圆二色谱（circular dichroism spectrum）估算其α螺旋（α helix）与β折叠股（β strand）的占比。计算所得结果已与Wang等人（2014）发表的HpDprA结构所计算得到的α螺旋占比与β折叠片（β sheet）占比进行对比。表征拟合优度的均方根偏差（RMSD）值已标注于括号内。
全长HpDprA及其单个结构域的二级结构组成。