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| Author(s): |
Jairo Cavalcante de Souza
Total Authors: 1
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| Document type: | Master's Dissertation |
| Press: | São Paulo. |
| Institution: | Universidade de São Paulo (USP). Instituto de Física (IF/SBI) |
| Defense date: | 2007-02-13 |
| Examining board members: |
Nelson Carlin Filho;
Jose Mestnik Filho;
Rajendra Narain Saxena
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| Advisor: | Nelson Carlin Filho |
| Field of knowledge: | Physical Sciences and Mathematics - Physics |
| Indexed in: | Banco de Dados Bibliográficos da USP-DEDALUS; Biblioteca Digital de Teses e Dissertações - USP |
| Location: | Universidade de São Paulo. Biblioteca do Instituto de Física; 539.7 M 2007; S729i |
| Abstract | |
This work is related to the implementation of a perturbed angular correlation (PAC) spectrometer at the University of São Paulo Pelletron Laboratory. The spectrometer consists of 6 cylindrical BaF$_2$ scintillator detectors, with 3 inches diameter and 6 inches length and a multiparameter CAMAC data acquisition system. Different from usual, the gamma ray energy spectra of the cascade nuclei are acquired for each detector, which allows us to have more control of the experiment. Besides, the same experiment can be revised with different approaches at any time. With the adopted electronics configuration, the energy spectra are obtained through a QDC (charge to digital converter) module, which dispenses the use of pre-amplifiers. The time spectra are acquired with a TDC (time to digital converter) module. The selection of coincidence events is performed computationally, and this procedure can be evaluated during the data acquisition. The main motivation for implementing this spectrometer is the study of the structure and interactions of biomolecules through the perturbed angular correlation technique. Test measurements were performed, parallel to the spectrometer construction, with the use of the Hyperfine Interactions Laboratory spectrometer at the Centro do Reator de Pesquisas do Instituto de Pesquisas Energéticas e Nucleares (CRPq-IPEN). The first measurements were performed with lipidic vesicles samples. In this case it was possible to observe the influence of the molecule dimension change (decrease in one order) on the rotational correlation time at room temperature, when SDS (sodium dodecyl sulfate) was added in the suspension to form micellar aggregation. The two following series of measurements were performed with SDS samples in which the concentration was varied in order to verify modifications in the geometry or mobility of the molecules as a function of that parameter. The behavior of the experimental perturbation functions varied with the samples. However, it was not possible to point out any systematics in their behavior. The molecules behavior when in presence of methanol in the samples was very different from the aqueous solutions. Also, it was not possible to obtain a clear conclusion about the critical micellar concentration for the aqueous solutions. Finally, the last measurements were performed with calmodulin protein samples, at room temperature and at 77K. In this case we concluded that this protein can be studied through the PAC technique. In order to confirm the presence of the protein in the samples and at same time to verify if any mass displacement occurred due to the presence of the $^{111}$Cd$^{2+}$, mass spectrometry measurements were performed at the Laboratório de Espectrometria de Massas -- Embrapa in Brasília. It was possible to confirm the presence of the protein in the samples, but it was not possible to observe the mass displacement due to the presence of the $^{111}$Cd, since the ions concentration used with the PAC technique is very low. (AU) | |