Difference between revisions of "Part:BBa K3561001"

Revision as of 13:54, 7 October 2020

Pd4 (Pacardo et al., 2009)

Pd4 is a palladium binding peptide. It is used as a library peptide in our project to act as a template for our mutations. The results of molecular dynamics for our modified peptides are also compared with this peptide. This peptide has an isoelectric point of 11.1, a molecular weight of 1.35 kDa and hydrophobicity of 21.38. The histidine residues at positions 6 and 11 are reported to bind to palladium and arginine is reported to coordinate with palladium in the literature of which the peptide is discovered(Pacardo et al., 2009). The serine and threonine residues at positions 1 and 2 are also reported to be important in binding with palladium(Sarikaya et al., 2003).

References: Pacardo, et al. “Biomimetic Synthesis of Pd Nanocatalysts for the Stille Coupling Reaction.” ACS Nano, U.S. National Library of Medicine, 2009, pubmed.ncbi.nlm.nih.gov/19422199/.

Sarikaya et al. “Molecular Biomimetics: Nanotechnology through Biology.” Nature News, Nature Publishing Group, 2003, www.nature.com/articles/nmat964.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

@@ Line 1: / Line 1: @@
 __NOTOC__
 <partinfo>BBa_K3561001 short</partinfo>
-Pd4 is a palladium binding peptide. It is used as a library peptide in our project to act as a template for our mutations. The results of molecular dynamics for our modified peptides are also compared with this peptide. This peptide has an isoelectric point of 11.1, a molecular weight of 1.35 kDa and hydrophobicity of 21.38. The histidine residues at positions 6 and 11 are reported to bind to palladium and arginine is reported to coordinate with palladium in the literature of which the peptide is discovered(Pacardo et al., 2009). The serine and threonine residues at positions 1 and 2 are also reported to be important in binding with palladium(2.	Sarikaya et al., 2003).
+Pd4 is a palladium binding peptide. It is used as a library peptide in our project to act as a template for our mutations. The results of molecular dynamics for our modified peptides are also compared with this peptide. This peptide has an isoelectric point of 11.1, a molecular weight of 1.35 kDa and hydrophobicity of 21.38. The histidine residues at positions 6 and 11 are reported to bind to palladium and arginine is reported to coordinate with palladium in the literature of which the peptide is discovered(Pacardo et al., 2009). The serine and threonine residues at positions 1 and 2 are also reported to be important in binding with palladium(Sarikaya et al., 2003).
+References:
+Pacardo, et al. “Biomimetic Synthesis of Pd Nanocatalysts for the Stille Coupling Reaction.” ACS Nano, U.S. National Library of Medicine, 2009, pubmed.ncbi.nlm.nih.gov/19422199/.
+Sarikaya et al. “Molecular Biomimetics: Nanotechnology through Biology.” Nature News, Nature Publishing Group, 2003, www.nature.com/articles/nmat964.
 <!-- Add more about the biology of this part here