Anthony Kennedy
Assistant Professor, Analytical Chemistry
- Principal Investigator, Walter Reed Army Institute of Research, Department of Blood Research, Maryland (2000-2007)
- Postdoctoral Fellow, Dublin Institute of Technology (2007)
- PhD, Chemistry, Trinity College Dublin (1996)
- BSc, Chemistry & Physics, Trinity College Dublin (1992)
Research in my group focuses primarily on the application of infrared spectroscopy for quantitative analysis. We are currently involved in several projects and details of two are given below.
Preservation of archaeological artifacts.
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Current work involves the determination of diffusion rates of preservatives into waterlogged archaeological wood taken from Beaufort Inlet Shipwreck (31CR314), believed to be Queen Anne's Revenge1, Blackbeard's pirate ship. These wooden artifacts cannot be dried or they will suffer excessive shrinkage and so the water within the remaining wood structure must be replaced in order to preserve the artifact. The current protocol (developed for preservation of the Vasa2 and the Mary Rose3) involves soaking the wood in polyethylene glycol (PEG-400) of various concentrations for several years. After several years of soaking the artifact may be lyophilized or soaked in PEG-4000 prior to long term storage or display.
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The Mary Rose during the preservation process |
It is important to ensure that the PEG is homogeneously dispersed within the wood and that a concentration profile does not exist, but conservators typically do not have the time or resources to monitor this, hence the excessive soaking times. Our goal is to make this process more efficient by determining the optimum soaking time for PEG that would produce the most consistent concentration of PEG throughout the entire piece of wood. We use simple gravimetric techniques and spectroscopic techniques for these studies.
1. http://www.qaronline.org/
2. http://www.vasamuseet.se/InEnglish/about.aspx
3. http://www.maryrose.org/
Protein and peptide secondary structure analysis.
Infrared spectroscopy may be used to determine protein and peptide secondary structure. The advantage of this technique over CD spectroscopy, NMR and crystallography is that conformational analysis reveals quantitative and qualitative data in a timely manner with small sample sizes. The secondary structure may also be analyzed in buffer which gives a more realistic picture of the protein or peptide in its native environment.
