Viroporin potential of the lentivirus lytic peptide (LLP) domains of the HIV-1 gp41 protein-3

<p><b>Copyright information:</b></p><p>Taken from "Viroporin potential of the lentivirus lytic peptide (LLP) domains of the HIV-1 gp41 protein"</p><p>http://www.virologyj.com/content/4/1/123</p><p>Virology Journal 2007;4():123-123.</p><p>Published online 20 Nov 2007</p><p>PMCID:PMC2211469.</p><p></p>unilamellar vesicles (LUV's) containing entrapped terbium and external DPA by LLP peptides is indicated by green Tb/DPA fluorescence under UV illumination

Viroporin potential of the lentivirus lytic peptide (LLP) domains of the HIV-1 gp41 protein-4

<p><b>Copyright information:</b></p><p>Taken from "Viroporin potential of the lentivirus lytic peptide (LLP) domains of the HIV-1 gp41 protein"</p><p>http://www.virologyj.com/content/4/1/123</p><p>Virology Journal 2007;4():123-123.</p><p>Published online 20 Nov 2007</p><p>PMCID:PMC2211469.</p><p></p> cylinders show the locations of the LLP domains. A hydrophibicity score could not be calculated for the entire LLP-1 domain due to its location at the extreme c-terminus of TM. (B) Helical wheel diagrams showing the amphipathic nature of each LLP domain. The coloring scheme is from Benner et al. and graphs were generated using a java applet [72]. (C) Primary amino acid sequence of the synthesized peptides used in subsequent experiments which correspond to the LLP-1, -2, and -3 domains of the TM protein

Viroporin potential of the lentivirus lytic peptide (LLP) domains of the HIV-1 gp41 protein-1

<p><b>Copyright information:</b></p><p>Taken from "Viroporin potential of the lentivirus lytic peptide (LLP) domains of the HIV-1 gp41 protein"</p><p>http://www.virologyj.com/content/4/1/123</p><p>Virology Journal 2007;4():123-123.</p><p>Published online 20 Nov 2007</p><p>PMCID:PMC2211469.</p><p></p>ce of 90%POPC:10%POPG (filled squares). Spectroscopic analysis revealed that each peptide possessed the characteristic minima at 208 nm and 222 nm indicating α-helical character. (a) LLP-1 labeled with NBD; (b) LLP-2 labeled with NBD; (c) LLP-3; (d) LLP-1D labeled with NBD. (e) The percent α-helicity was calculated from the CD spectroscopy curves in figure a-d for each peptide using the following formula: Θ/(1–2.5/n)(40,000), where n = the number of residues present in the peptide

Viroporin potential of the lentivirus lytic peptide (LLP) domains of the HIV-1 gp41 protein-5

<p><b>Copyright information:</b></p><p>Taken from "Viroporin potential of the lentivirus lytic peptide (LLP) domains of the HIV-1 gp41 protein"</p><p>http://www.virologyj.com/content/4/1/123</p><p>Virology Journal 2007;4():123-123.</p><p>Published online 20 Nov 2007</p><p>PMCID:PMC2211469.</p><p></p>ce of 90%POPC:10%POPG (filled squares). Spectroscopic analysis revealed that each peptide possessed the characteristic minima at 208 nm and 222 nm indicating α-helical character. (a) LLP-1 labeled with NBD; (b) LLP-2 labeled with NBD; (c) LLP-3; (d) LLP-1D labeled with NBD. (e) The percent α-helicity was calculated from the CD spectroscopy curves in figure a-d for each peptide using the following formula: Θ/(1–2.5/n)(40,000), where n = the number of residues present in the peptide

Viroporin potential of the lentivirus lytic peptide (LLP) domains of the HIV-1 gp41 protein-0

<p><b>Copyright information:</b></p><p>Taken from "Viroporin potential of the lentivirus lytic peptide (LLP) domains of the HIV-1 gp41 protein"</p><p>http://www.virologyj.com/content/4/1/123</p><p>Virology Journal 2007;4():123-123.</p><p>Published online 20 Nov 2007</p><p>PMCID:PMC2211469.</p><p></p> cylinders show the locations of the LLP domains. A hydrophibicity score could not be calculated for the entire LLP-1 domain due to its location at the extreme c-terminus of TM. (B) Helical wheel diagrams showing the amphipathic nature of each LLP domain. The coloring scheme is from Benner et al. and graphs were generated using a java applet [72]. (C) Primary amino acid sequence of the synthesized peptides used in subsequent experiments which correspond to the LLP-1, -2, and -3 domains of the TM protein