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Construction Of An Instrument For Doing Fast Time-Resolved Infrared Spectroscopy, Susan R. Richter
Construction Of An Instrument For Doing Fast Time-Resolved Infrared Spectroscopy, Susan R. Richter
Honors Theses
We have designed and assembled a system for doing flash photochemical studies of organotransition metal carbonyl complexes with fast time-resolved infrared detection. Photolysis is with conventional xenon flashlamps (400J/flash) and time resolved infrared absorption spectra are measured with a diode laser (Laser Photonics, Inc.) and indium antimonide detector operating in the range 1700 - 2100 cm -1. Signals are collected and averaged on a digital oscilloscope (LeCroy 9410) for subsequent computer storage and analysis. The waveform is downloaded to the computer where calculations of percent transmittance and absorbance vs time are calculated. The information is then transferred to a spreadsheet …
Evaluation Of The Pti Ls-100 Lifetime Instrument And The Binding Of 2-Acetylnaphthalene To Γ-Cyclodextrins And Modified Β-Cyclodextrins, Timothy R. Cregan
Evaluation Of The Pti Ls-100 Lifetime Instrument And The Binding Of 2-Acetylnaphthalene To Γ-Cyclodextrins And Modified Β-Cyclodextrins, Timothy R. Cregan
Honors Theses
The first part of this thesis is to determine the procedures for optimizing the data obtained from the PTI LS-100 lifetime instrument. The molecules 9-cyanoanthracene, pyrenebutyric acid, anthracene and N-acetyltrytophanamide have lifetimes which vary over the range 1 to 115 nsec and all follcw a s:ngle exponential decay. Therefore, we can evaluate the instrument by comparing these data using fluorescence lifetime reference standard values for the aforementioned molecules. The second part of this thesis is to investigate the binding of 2-acetylnaphthalere (2-AN) to various cyclodextrin molecules.
Tyrosine Flourescence To Monitor The Denaturation Of A Bacterial Protein, Kristin L. Trudeau
Tyrosine Flourescence To Monitor The Denaturation Of A Bacterial Protein, Kristin L. Trudeau
Honors Theses
Tyrosine fluorescence was used to monitor the denaturation of a protein. The protein used as our model system was the regulatory subunit (RSU) of aspartate transcarbamoylase from E. coli. RSU is a dimer of two identical chains with one zinc ion bound per chain. It is also a typtophan-deficient protein so tyrosine flourescence was used as a probe to monitor changes during denaturation.
Denaturation Studies On Aspartate Transcarbamoylase And Its Catalytic Subunit, Neil B. Grodsky
Denaturation Studies On Aspartate Transcarbamoylase And Its Catalytic Subunit, Neil B. Grodsky
Honors Theses
Two separate but overlapping projects were studied. First, the tryptophan corrected fluorescence emission spectra of ATCase and CSU were characterized under a variety of denaturant conditions at excitation 295 nm. Because CSU is a portion of ATCase, the environments of the same two tryptophan residues were being probed in both systems.