Secondary Structure Analysis

YL Yue Liu
DS Daning Shi
JW Jin Wang
XC Xiaoling Chen
MZ Mei Zhou
XX Xinping Xi
JC Jianming Cheng
CM Chengbang Ma
TC Tianbao Chen
CS Chris Shaw
LW Lei Wang
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The secondary structure of the peptide was determined by use of circular dichroism spectrometry (JASCO J-815 CD spectrometer, Jasco, Essex, United Kingdom) as described in a previous study (Gao et al., 2016; Wu et al., 2016). Peptides were dissolved in 10 mM ammonium acetate buffer or 50% TFE in 10 mM ammonium acetate buffer at a final concentration of 100 μM. The percentage of the α-helix structure was predicted by the online tool K2D3 (Louis-Jeune et al., 2012). Peptide samples were measured within the range of 190–250 nm at 20°C. The parameters were set as: 200 nm/min scanning speed, a bandwidth of 1 nm, and 0.5 nm data pitch.

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