Tachyplesin: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Janak Raj Joshi, Shulamit Idzikowski, Michal Harel, Alexander Berchansky, Joel L. Sussman, Angel Herraez, Jaime Prilusky

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 The β-hairpin topology of CDT is sustained by the <scene name='67/671725/Cdthaipin/2'>unique packing interactions</scene> between the aromatic ring of Trp2 and the side-chain of nonpolar amino acid of Val5 and the cationic side-chain of residue Arg11.
 Also, there exists close proximity between residues <scene name='67/671725/Cdtnoe/1'>Trp2 and Ile9</scene> which is supported by [http://en.wikipedia.org/wiki/Nuclear_Overhauser_effect nuclear overhauser effects (NOEs)] involving [http://en.wikipedia.org/wiki/Indole indole] ring protons of Trp2 with side-chain proton of Ile9. These packing interactions have rendered an approximate anti-parallel orientation of the hairpin structure of CDT in presence of LPS.
-The β-hairpin like structure of CDT displays an extended <font color='darkblue'>positively charged</font> surface patch of <scene name='67/671725/Cdtr4r7r12r13/1'>residues Arg 4, 7, 12 and 13</scene>. These positively charged basic residues interacts with the anionic phosphate groups of LPS, that leads to a plausible disruption or fluidization of LPS structures. This facilitates traversal of the peptide through the LPS-outer membrane<ref name=Saravanan>PMID:22464970</ref>.
+The β-hairpin structure displays an extended <font color='darkblue'>positively charged</font> surface patch of <scene name='67/671725/Cdtr4r7r12r13/1'>residues Arg 4, 7, 12 and 13</scene>. These positively charged basic residues interacts with the anionic phosphate groups of LPS, that leads to a plausible disruption or fluidization of LPS structures. This facilitates traversal of the peptide through the LPS-outer membrane<ref name=Saravanan>PMID:22464970</ref>.