The studies developed throughout this work are applicable to both areas. In this context, the present thesis presents the use of different mathematical techniques to deal with different various and current problems in astrodynamics and celestial mechanics. From the physical understanding of the motion of celestial bodies to the planing and designing of space missions, the use of mathematical models to deal with a very large number of contemporary problems plays a fundamental role in the progress of human knowledge. Nowadays, despite the technological development experienced by science in general, a fact especially evident by the available powerful computer machines, the analytical and semi-analytical methods to study different space problems are still of great importance in the fields of astrodynamics and celestial mechanics.

of bitstreams: 1įundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Tese_Final_Josue_Cardoso_Santos.pdf: 78449557 bytes, checksum: 4515b9cb7cc346753f7e9682b8e037de (MD5)Īpproved for entry into archive by Pamella Benevides Gonçalves null on (GMT) No. Submitted by Josué Cardoso dos Santos on These new set of tools were applied for the first time to the study of Flavin Adenine Dinucleotide (FAD), Nicotineamide Adenine Dinucleotide (NAD), globular protein cytochrome c (cyt c), the 31 knot YibK protein, 52 knot ubiquitin C terminal hydrolase (UCH) protein, and the 61 knot halo acid dehydrogenase (DehI) protein. When coupled to mass spectrometry (TIMS-MS), action spectroscopy (IRMPD), molecular dynamics and biochemical approaches (e.g., fluorescence lifetime spectroscopy), a comprehensive description of the biomolecules dynamics and tridimensional structural can be obtained. In the present work, we pioneered the application of a new variant of ion mobility spectrometry, trapped ion mobility spectrometry (TIMS), which provides high mobility resolving power and the possibility to study kinetically trapped intermediates as a function of the starting solution (e.g., pH and organic content) and gas-phase conditions (e.g., collisional activation, molecular dopants, hydrogen/deuterium back-exchange). As an alternative, complementary tools that can capture and sample multiple conformations needed to be developed. Many biomolecular systems adopt multiple structures as a function of their microenvironment, which makes them difficult to be characterized by traditional structural biology tools (e.g., NMR, X-ray crystallography).

One of the main goals in structural biology is to understand the folding mechanisms and three-dimensional structure of biomolecules.

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