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Tachyplesin
From Proteopedia
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There are three linear derivatives: <scene name='67/671725/1ma4/1'>TPY4</scene>, TPF4 and TPA4. | There are three linear derivatives: <scene name='67/671725/1ma4/1'>TPY4</scene>, TPF4 and TPA4. | ||
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 presence of LPS. The backbone of the polypeptide becomes more rigid and twisted in presence of LPS, making it more stable. | + | 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 more rigid and twisted in presence of LPS, making it more stable. |
== Importance == | == Importance == | ||
Revision as of 14:22, 26 December 2014
Introduction
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References
Proteopedia Page Contributors and Editors (what is this?)
Shulamit Idzikowski, Janak Raj Joshi, Michal Harel, Alexander Berchansky, Joel L. Sussman, Angel Herraez, Jaime Prilusky
