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Doctoral Thesis
DOI
10.11606/T.54.1984.tde-19082014-100219
Document
Author
Full name
Joao Ruggiero Neto
Institute/School/College
Knowledge Area
Date of Defense
Published
São Carlos, 1984
Supervisor
Committee
Tabak, Marcel (President)
Lamy, Maria Teresa Moura
Louro, Sonia Renaux Wanderley
Nascimento, Otaciro Rangel
Sanches, Rosemary
Title in Portuguese
Interação de pequenas moléculas com proteínas: um estudo usando métodos convencionais e transferência de saturação de R.P.E.
Keywords in Portuguese
Hemoglobina
Interação proteína
Moléculas pequenas
RPE
TS-RPE
Abstract in Portuguese
Neste trabalho, analisamos a interação de pequenas moléculas, marcadores hidrofóbicos, com hemoglobina, em diferentes estados: monocristal, pó e solução aquosa. Os métodos de análise empregados, são baseados nas teorias de relaxação em líquidos e técnicas não lineares de ressonância ST-RPE (transferência de saturação), fornecendo informações sobre mudanças locais nas vizinhanças desses marcadores. Um dos marcadores hidrofóbicos, o TEMPO, mostrou uma anisotropia considerável nos espectros de RPE do monocristal de hemoglobina que está relacionado com o empacotamento molecular da proteína do cristal. A associação desses métodos de análise conduziu a importantes informações sobre mudanças na camada de hidratação em várias proteínas: hemoglobina, mioglobina e lisozima, monitoradas pelo marcador covalente derivado da maleimida, e induzidas pela temperatura, sob diferentes condições de hidratação. Desta forma o uso da espectroscopia de RPE especialmente com simulação espectral e DT-RPE mostro ser um método potente e ainda não explorado no estado de hidratação de proteínas
Title in English
On the interaction of small molecules with proteins: a conventional EPR and ST-EPR study
Keywords in English
EPR
Hemoglobin
Protein interaction
Small molecules
ST-EPR
Abstract in English
In this work, the interactions of small molecules, hydrophobic spin labels, with hemoglobin, under different states was analysed: single crystal, powder and aqueous solution. The methods of analysis employed, are based in relaxation theory in liquids and non-linear techniques, saturation transfer (ST-EPR), giving informations on the local changes in neighbourhood of the labels. One of the hydrophobic labels, TEMPO, showed a considerable anisotropy in the hemoglobin single crystal spectra, a result related to the molecular packing in the protein single crystal. The association of the techniques of analysis all together lead to important informations an temperature induced changes in the hydration layer in several proteins: hemoglobin, myoglobin, NEM*, a maleimide derivated, in different conditions of hydration. In this way the use of EPR spectroscopy and particularly with spectral simulations and ST-EPR, proved to be a powerful and not yet very much explored method to study the problem of protein hydration
 
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JoaoRuggieroNetoD.pdf (6.23 Mbytes)
Publishing Date
2014-08-21
 
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