Sandbox GGC9: Difference between revisions

Line 13:

The collagen complex with binding protein represent in this <scene name='75/752271/Collagenadhesincomplex/2'>view</scene>. Furthermore, this <scene name='75/752271/Procollagen/1'>Ttriple helices</scene> represents the structure of procollagen (triple α-chain). The structural of hydroxyproline redisue of <scene name='75/752271/Hypresidue/2'>Hydroxylproline</scene>.

~~Refer~~ back to the the collagen-binding site of human Type I and Type III collagen, VWF-A3 is distinctly different from that of the homologous integrin α2 I domain, which ~~has~~ a hydrophilic binding site located at the top face of the domain. Based on the surface characteristics of the collagen-binding site, the proposal is that collagen-binding protein interact with collagen sequences containing positively charged and hydrophobic residues. The <scene name='75/752271/Procollagenii/1'>particular amino acid residues</scene>s in the binding protein in this case CNA interact with the residue of the collagen base on the polarity and non-polar molecules. Therefore, bacterial adhesion follows the same rule as eukaryotic binding factors.

Refering back to the the collagen-binding site of human Type I and Type III collagen, VWF-A3 is distinctly different from that of the homologous integrin α2 I domain, in which contains a hydrophilic binding site located at the top face of the domain. Based on the surface characteristics of the collagen-binding site, the proposal is that collagen-binding protein interact with collagen sequences containing positively charged and hydrophobic residues. The <scene name='75/752271/Procollagenii/1'>particular amino acid residues</scene>s in the binding protein in this case CNA interact with the residue of the collagen base on the polarity and non-polar molecules. Therefore, bacterial adhesion follows the same rule as eukaryotic binding factors. Bacteria CNA protein then wraps around the collagen active site and slightly tighten it with its CNA protein residue.

== References ==

Sandbox GGC9: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 13: / Line 13: @@
 The collagen complex with binding protein represent in this <scene name='75/752271/Collagenadhesincomplex/2'>view</scene>. Furthermore, this <scene name='75/752271/Procollagen/1'>Ttriple helices</scene> represents the structure of procollagen (triple α-chain). The structural of hydroxyproline redisue of <scene name='75/752271/Hypresidue/2'>Hydroxylproline</scene>.
-Refer back to the the collagen-binding site of human Type I and Type III collagen, VWF-A3 is distinctly different from that of the homologous integrin α2 I domain, which has a hydrophilic binding site located at the top face of the domain. Based on the surface characteristics of the collagen-binding site, the proposal is that collagen-binding protein interact with collagen sequences containing positively charged and hydrophobic residues. The <scene name='75/752271/Procollagenii/1'>particular amino acid residues</scene>s in the binding protein in this case CNA interact with the residue of the collagen base on the polarity and non-polar molecules. Therefore, bacterial adhesion follows the same rule as eukaryotic binding factors.
+Refering back to the the collagen-binding site of human Type I and Type III collagen, VWF-A3 is distinctly different from that of the homologous integrin α2 I domain, in which contains a hydrophilic binding site located at the top face of the domain. Based on the surface characteristics of the collagen-binding site, the proposal is that collagen-binding protein interact with collagen sequences containing positively charged and hydrophobic residues. The <scene name='75/752271/Procollagenii/1'>particular amino acid residues</scene>s in the binding protein in this case CNA interact with the residue of the collagen base on the polarity and non-polar molecules. Therefore, bacterial adhesion follows the same rule as eukaryotic binding factors. Bacteria CNA protein then wraps around the collagen active site and slightly tighten it with its CNA protein residue.
 == References ==