Banca de QUALIFICAÇÃO: ISABELLE ALVES PEREIRA

Uma banca de QUALIFICAÇÃO de MESTRADO foi cadastrada pelo programa.
STUDENT : ISABELLE ALVES PEREIRA
DATE: 31/07/2025
TIME: 09:00
LOCAL: https://conferenciaweb.rnp.br/sala/Qualifica-Isabelle
TITLE:

Brazilian Variants of the SARS-CoV-2 Virus: An Analysis of the Effect of Mutations on Spike and ACE 2 Interactions

PAGES: 60
BIG AREA: Ciências Biológicas
AREA: Biofísica
SUBÁREA: Biofísica Molecular
SUMMARY:

In December 2019, a novel disease, initially referred to as pneumonia of unknown cause, began spreading rapidly in Wuhan, China, causing symptoms such as dry cough, headache, fever, chest discomfort, sore throat, and respiratory insufficiency in the population [. On December 31st, the World Health Organization (WHO) was notified. By March 11th, 2020, the disease, by then called COVID-19, was declared a global public health emergency and a pandemic. COVID-19 is caused by Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), a betacoronavirus from the Coronaviridae family, similar to SARS-CoV (2002) [4] and MERS-CoV (2012) [2], both known for causing severe respiratory diseases. SARS-CoV-2 is a single-stranded RNA virus with a large genome. It encodes two large polyproteins, four structural proteins, and nine accessory proteins [5,6]. The genome follows a 5’-3’ arrangement in the following order: replicase (ORF1a/ORF1b), Spike (S), Envelope (E), Membrane (M), and the Nucleocapsid (N), which is located inside the viral particle along with the RNA Structural dynamics play essential roles in signaling, catalysis, and other fundamental activities in cells. Characterizing the full ensemble of conformations visited by a given macromolecular system is therefore essential to deciphering their functional role and such studies require both experimental and computational efforts. This work aims to study the structural plasticity and dynamics of the glycoprotein spike of SARS-COV-2 using Molecular Dynamics, Normal Modes all atoms, Elastic Network Models and Machine Learning techniques  to compare the results with what is known in the literature. Our research hypothesis is that conformational changes, dynamics and transient conformations are critically important for protein function, yet methods to map out pathways and identify transient structures lag behind the methods used for structure determination of well-populated stable states.

COMMITTEE MEMBERS:
Presidente - Interno ao Programa - 1563992 - ANA LIGIA BARBOUR SCOTT
Membro Titular - Examinador(a) Externo à Instituição - LÍVIA DE MORAES BOMEDIANO CAMILLO
Membro Titular - Examinador(a) Externo à Instituição - RAFAEL PLANA SIMÕES - UNESP
Membro Suplente - Examinador(a) Interno ao Programa - 2605420 - MARIA CRISTINA CARLAN DA SILVA