Tachyplesin: Difference between revisions
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TP-I undergoes a conformational change in the <scene name='67/671725/Tp_i_in_the_presence_of_lps/1'>presence of LPS </scene>. The backbone of the polypeptide becomes <scene name='67/671725/Conformation_change/8'>more rigid and twisted in the presence of LPS, than in the presence of water</scene>, making it more stable. | TP-I undergoes a conformational change in the <scene name='67/671725/Tp_i_in_the_presence_of_lps/1'>presence of LPS </scene>. The backbone of the polypeptide becomes <scene name='67/671725/Conformation_change/8'>more rigid and twisted in the presence of LPS, than in the presence of water</scene>, making it more stable. | ||
Along with the requirement for β-hairpin conformation, there is a second requirement for activity and it is the ability to rearrange to a more amphiphilic conformation upon membrane association. | |||
In the wild type | |||