3p4z: Difference between revisions

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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>  
[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>  
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== Publication Abstract from PubMed ==
Gold nanoparticles are useful in biomedical applications due to their distinct optical properties and high chemical stability. Reports of the biogenic formation of gold colloids from gold complexes has also led to an increased level of interest in the biomineralization of gold. However, the mechanism responsible for biomolecule-directed gold nanoparticle formation remains unclear due to the lack of structural information about biological systems and the fast kinetics of biomimetic chemical systems in solution. Here we show that intact single crystals of lysozyme can be used to study the time-dependent, protein-directed growth of gold nanoparticles. The protein crystals slow down the growth of the gold nanoparticles, allowing detailed kinetic studies to be carried out, and permit a three-dimensional structural characterization that would be difficult to achieve in solution. Furthermore, we show that additional chemical species can be used to fine-tune the growth rate of the gold nanoparticles.
Time-dependent, protein-directed growth of gold nanoparticles within a single crystal of lysozyme.,Wei H, Wang Z, Zhang J, House S, Gao YG, Yang L, Robinson H, Tan LH, Xing H, Hou C, Robertson IM, Zuo JM, Lu Y Nat Nanotechnol. 2011 Feb;6(2):93-7. Epub 2011 Jan 30. PMID:21278750<ref>PMID:21278750</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3p4z" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==

Latest revision as of 12:32, 30 October 2024

Time-dependent and Protein-directed In Situ Growth of Gold Nanoparticles in a Single Crystal of LysozymeTime-dependent and Protein-directed In Situ Growth of Gold Nanoparticles in a Single Crystal of Lysozyme

Structural highlights

3p4z is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LYSC_CHICK Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.[1]

Publication Abstract from PubMed

Gold nanoparticles are useful in biomedical applications due to their distinct optical properties and high chemical stability. Reports of the biogenic formation of gold colloids from gold complexes has also led to an increased level of interest in the biomineralization of gold. However, the mechanism responsible for biomolecule-directed gold nanoparticle formation remains unclear due to the lack of structural information about biological systems and the fast kinetics of biomimetic chemical systems in solution. Here we show that intact single crystals of lysozyme can be used to study the time-dependent, protein-directed growth of gold nanoparticles. The protein crystals slow down the growth of the gold nanoparticles, allowing detailed kinetic studies to be carried out, and permit a three-dimensional structural characterization that would be difficult to achieve in solution. Furthermore, we show that additional chemical species can be used to fine-tune the growth rate of the gold nanoparticles.

Time-dependent, protein-directed growth of gold nanoparticles within a single crystal of lysozyme.,Wei H, Wang Z, Zhang J, House S, Gao YG, Yang L, Robinson H, Tan LH, Xing H, Hou C, Robertson IM, Zuo JM, Lu Y Nat Nanotechnol. 2011 Feb;6(2):93-7. Epub 2011 Jan 30. PMID:21278750[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
  2. Wei H, Wang Z, Zhang J, House S, Gao YG, Yang L, Robinson H, Tan LH, Xing H, Hou C, Robertson IM, Zuo JM, Lu Y. Time-dependent, protein-directed growth of gold nanoparticles within a single crystal of lysozyme. Nat Nanotechnol. 2011 Feb;6(2):93-7. Epub 2011 Jan 30. PMID:21278750 doi:10.1038/nnano.2010.280

3p4z, resolution 1.60Å

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