Estudo da estabilidade estrutural em solução aquosa da enzima Acetolactato Sintase (ALS) utilizando Dinâmica Molecular

• Autor(a) principal: Paula, Guilherme Augusto Pinheiro de
• Data de Publicação: 2019
• Tipo de documento: Trabalho de conclusão de curso
• Idioma: por
• Título da fonte: Repositório Institucional da UFU
• Texto Completo: https://repositorio.ufu.br/handle/123456789/26042
• topic: Enzima; ALS; AHAS; TPP; FAD; Dinâmica molecular; Estabilidade estrutural; CNPQ::CIENCIAS EXATAS E DA TERRA::QUIMICA::FISICO-QUIMICA::QUIMICA TEORICA

This undergraduate thesis aims to study the enzymatic dimer structure of the enzyme Acetolactate Synthase (ALS) and its structural conformation with the presence and absence of its cofactors: Flavin adenine dinucleotide (FAD) and Thiamine pyrophosphate (TPP), whose according to the literature has the function of assist the stability of the enzyme and also a role in the enzymatic process. In order to shed light to these answers, atomistic Molecular Dynamics simulations, in the ensemble NPT, were carried in aqueous solution, to obtain knowledge enough to make a nanobiosensor with atomic microscopy force (AFM). The results showed that the cofactors FAD and TPP do not affect significantly the enzyme conformation on the hydrogen bond pattern of the system.