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. | 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 TP-I,<scene name='67/671725/Conformation_change/9'> Arg 5 and Arg 14</scene>, Provides this by acting as hinges. | In the wild type TP-I,<scene name='67/671725/Conformation_change/9'> Arg 5 and Arg 14</scene>, Provides this by acting as hinges.<ref name=Laederach>PMID:12369825</ref> | ||
