Tachyplesin: Difference between revisions
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The amino acid sequence of the TP-I is NH₂-Lys-Trp-Cys-Phe-Arg-Val-Cys-Tyr-Arg-Gly-Ile-Cys-Tyr-Arg-Arg-Cys-Arg-CONH₂. | The amino acid sequence of the TP-I is NH₂-Lys-Trp-Cys-Phe-Arg-Val-Cys-Tyr-Arg-Gly-Ile-Cys-Tyr-Arg-Arg-Cys-Arg-CONH₂. | ||
[[Image:scheme1.jpg|150px|left|thumb|<b>Figure 1: Simplified model of Tachyplesin I.</b>]] | [[Image:scheme1.jpg|150px|left|thumb|<b>Figure 1: Simplified model of Tachyplesin I.</b>]] | ||
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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, Arg 5 and Arg 14, 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. | ||
