Tachyplesin: Difference between revisions
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Since linear tachyplesin analogues do not show preferential affinity for LPS, the hairpin properties of the peptide seems to be important for recognition of lipopolysaccharides and its biological activities. | Since linear tachyplesin analogues do not show preferential affinity for LPS, the hairpin properties of the peptide seems to be important for recognition of lipopolysaccharides and its biological activities. | ||
TPI undergoes confirmation change in <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/ | TPI undergoes confirmation change in <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/3'>more rigid and twisted in presence of LPS, than in the presence of water </scene>, making it more stable. | ||
== Mode of action == | == Mode of action == | ||
