Tachyplesin: Difference between revisions

Line 15:

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.

The two β-strands slightly extends when TP-I binds to LPS and stabilize the whole structure of TP-I as a result.

Fluorescence studies indicate that the Trp residue incorporated into the hydrophobic environment of LPS. [http://en.wikipedia.org/wiki/Nuclear_magnetic_resonance NMR] studies suggest that residues located in the N and C termini of TP-I are involved in the binding to LPS and that phosphate groups of LPS are in close proximity to TP-I. <ref name=Kushibiki>PMID:24389234</ref>

Fluorescence studies indicate that the <scene name='67/671725/Conformation_change/10'>Trp residue</scene> incorporated into the hydrophobic environment of LPS. [http://en.wikipedia.org/wiki/Nuclear_magnetic_resonance NMR] studies suggest that residues located in the N and C termini of TP-I are involved in the binding to LPS and that phosphate groups of LPS are in close proximity to TP-I. <ref name=Kushibiki>PMID:24389234</ref>

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.

Tachyplesin: Difference between revisions

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@@ Line 15: / Line 15: @@
 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.
 The two β-strands slightly extends when TP-I binds to LPS and stabilize the whole structure of TP-I as a result.
-Fluorescence studies indicate that the Trp residue incorporated into the hydrophobic environment of LPS. [http://en.wikipedia.org/wiki/Nuclear_magnetic_resonance NMR] studies suggest that residues located in the N and C termini of TP-I are involved in the binding to LPS and that phosphate groups of LPS are in close proximity to TP-I. <ref name=Kushibiki>PMID:24389234</ref>
+Fluorescence studies indicate that the <scene name='67/671725/Conformation_change/10'>Trp residue</scene> incorporated into the hydrophobic environment of LPS. [http://en.wikipedia.org/wiki/Nuclear_magnetic_resonance NMR] studies suggest that residues located in the N and C termini of TP-I are involved in the binding to LPS and that phosphate groups of LPS are in close proximity to TP-I. <ref name=Kushibiki>PMID:24389234</ref>
 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.