User:Michael F. Nagle/Notebook/Chem 571/2012/09/04: Difference between revisions
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==Data== | ==Data== | ||
Data for mole ratios from 130-140 was lost. This is because all spectra were saved as data print tables once trials were complete, and the spectra from 130-140 were not double clicked on before "Save" was clicked, and so other spectra were saved in their place. They could not be retrieved since the .spc files were not backed up. | |||
[[Image: | [[Image:AuBSA1.png]] | ||
==Discussion== | ==Discussion== | ||
* | * A significant drop in absorbance is seen between mole ratios 120 and 128. This indicates that this may be the point where gold nanoparticles stop going into solution and are only in fibers. However, research by Bakshi, et. al.<sup>1</sup>, indicates that the optimal mole ratio is from 132-134. More trials are needed to determine where the optimal range is. | ||
*Dissolution of fibers in Tris should be tested at pH's 8 and 10 because Tris's optimal range is 7-9. | *Dissolution of fibers in Tris should be tested at pH's 8 and 10 because Tris's optimal range is 7-9. We will also replicate previous experiments that used a pH of 10. | ||
References | |||
Bakshi, M.S.; Kaur, H.; Khullar, P.; Banipal, T. S.l; Kaur, G.; Singh, N. Protein Films of Bovine Serum Albumen Conjugated Gold Nanoparticles: A Synthetic Route from Bioconjugated Nanoparticles to Biodegradable Protein Films.<i> J. Phys. Chem.</i> C, 2011, 115 (7), pp 2982–2992 | |||
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Objective
Procedure
DataData for mole ratios from 130-140 was lost. This is because all spectra were saved as data print tables once trials were complete, and the spectra from 130-140 were not double clicked on before "Save" was clicked, and so other spectra were saved in their place. They could not be retrieved since the .spc files were not backed up. Discussion
References Bakshi, M.S.; Kaur, H.; Khullar, P.; Banipal, T. S.l; Kaur, G.; Singh, N. Protein Films of Bovine Serum Albumen Conjugated Gold Nanoparticles: A Synthetic Route from Bioconjugated Nanoparticles to Biodegradable Protein Films. J. Phys. Chem. C, 2011, 115 (7), pp 2982–2992 |