Tachyplesin: Difference between revisions
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[http://en.wikipedia.org/wiki/Nuclear_magnetic_resonance NMR] studies have shown that TP-I undergoes a conformational change from <scene name='67/671725/First_scene/5'>water surrounding</scene> to <scene name='67/671725/Tp_i_in_the_presence_of_lps/4'>presence of LPS</scene>, making it <scene name='67/671725/Conformation_change/16'>more rigid and twisted</scene> than in the presence of water<ref name=Kushibiki>PMID:24389234</ref>. Moreover a docking model suggests the stability of the structure of TP-I is increased in the presence of LPS by the binding of the N and C termini of TP-I to LPS. The conformational change of TP-I seems to be crucial for its antimicrobial activity, since rearrangement of TP-I structure makes it more amphiphilic to negatively charged membrane of bacteria and fungus<ref name=Laederach>PMID:12369825</ref>. | [http://en.wikipedia.org/wiki/Nuclear_magnetic_resonance NMR] studies have shown that TP-I undergoes a conformational change from <scene name='67/671725/First_scene/5'>water surrounding</scene> to <scene name='67/671725/Tp_i_in_the_presence_of_lps/4'>presence of LPS</scene>, making it <scene name='67/671725/Conformation_change/16'>more rigid and twisted</scene> than in the presence of water<ref name=Kushibiki>PMID:24389234</ref>. Moreover a docking model suggests the stability of the structure of TP-I is increased in the presence of LPS by the binding of the N and C termini of TP-I to LPS. The conformational change of TP-I seems to be crucial for its antimicrobial activity, since rearrangement of TP-I structure makes it more amphiphilic to negatively charged membrane of bacteria and fungus<ref name=Laederach>PMID:12369825</ref>. | ||