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    Changes On The Structural Dynamics of Mpro (Sars-Cov-2) Influencing The Substrate Bindings and Catalytic Mechanism

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    Yolanda Marcello
    The document discusses changes in the structural dynamics of Mpro (SARS-CoV-2 main protease) and how those changes influence substrate binding and catalytic mechanism. It analyzes wild-type and mutant forms of Mpro using normal modes analysis and molecular dynamics simulations to study flexibility. Molecular docking was also used to show two mutants allow better substrate docking and more stable complexes. Physical-chemical analysis of substrates helped understand the peptide binding profile and molecular interactions important for catalytic activity.

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    Changes On The Structural Dynamics of Mpro (Sars-Cov-2) Influencing The Substrate Bindings and Catalytic Mechanism

    Uploaded by

    Yolanda Marcello
    12 views1 page
    The document discusses changes in the structural dynamics of Mpro (SARS-CoV-2 main protease) and how those changes influence substrate binding and catalytic mechanism. It analyzes wild-type and mutant forms of Mpro using normal modes analysis and molecular dynamics simulations to study flexibility. Molecular docking was also used to show two mutants allow better substrate docking and more stable complexes. Physical-chemical analysis of substrates helped understand the peptide binding profile and molecular interactions important for catalytic activity.

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    Changes on the Structural Dynamics of Mpro (Sars-Cov-2 ) Influencing the Substrate Bindings and Catalytic Mechanism

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    The document discusses changes in the structural dynamics of Mpro (SARS-CoV-2 main protease) and how those changes influence substrate binding and catalytic mechanism. It analyzes wild-type and mutant forms of Mpro using normal modes analysis and molecular dynamics simulations to study flexibility. Molecular docking was also used to show two mutants allow better substrate docking and more stable complexes. Physical-chemical analysis of substrates helped understand the peptide binding profile and molecular interactions important for catalytic activity.

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    © All Rights Reserved
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    12 views1 page

    Changes On The Structural Dynamics of Mpro (Sars-Cov-2) Influencing The Substrate Bindings and Catalytic Mechanism

    Uploaded by

    Yolanda Marcello
    The document discusses changes in the structural dynamics of Mpro (SARS-CoV-2 main protease) and how those changes influence substrate binding and catalytic mechanism. It analyzes wild-type and mutant forms of Mpro using normal modes analysis and molecular dynamics simulations to study flexibility. Molecular docking was also used to show two mutants allow better substrate docking and more stable complexes. Physical-chemical analysis of substrates helped understand the peptide binding profile and molecular interactions important for catalytic activity.

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    of 1

    CHANGES ON THE STRUCTURAL DYNAMICS OF MPRO (SARS-COV-2 )

    INFLUENCING THE SUBSTRATE BINDINGS AND CATALYTIC


    MECHANISM
    Marcello, Y. M. B. *; Pantaleão, S. Q.*; Gasparini, P.* ; Philot, E. A.*; Simões, R. P.**; Magro, A. J.***; Scott, A. L.*

    *Computational Biology and Biophysics Laboratory, UFABC, Santo André, SP, Brazil; **Department of Bioprocesses and Biotechnology, School of
    Agriculture, Unesp, Botucatu, SP, Brazil; ***Institute of Biotechnology, Unesp, Botucatu, SP, Brazil.

    INTRODUCTION RESULTS
    Macromolecules adopt several favored conformations in solution The docking analysis results showed that there are two mutants
    depending on their structure, determining their that allow a better docking and produce more stable complexes.
    dynamics/function. In a previous work, we compared the wild- Mapping the key points of the peptide structure with biological
    type and single-point mutant SARS--CoV-2 Mpro using a action on Mpro through physical-chemical characterization,
    normal modes (NM) based protocol to analyze simple makes it possible to understand the peptide profile, together with
    parameters such as Cα flexibility (Gasparini et. al, 2023). It has the study of molecular docking and essential molecular impulses
    been investigated how these mutations on Mpro (K90R, P99L, for the protein reflex.
    P108S, and N151D) can influence the catalytic mechanism.
    Figure 1 -

    OBJECTIVES
    We intend to continue this work studying how changes on the
    structural dynamics of the protein can influenceIthe substrate
    binding and the catalytic mechanism.

    METODOLOGY

    First step:
    Normal First step: physical-chemical

    Modes

    (NM) properties

    analysis
    Figure 2 -
    Second
    step:

    Molecular
    Dymaics Second step:

    with VMOD toxicity,


    hydrophobicity,
    sterichinderance

    Protease

    structure

    substrates
    analysis
    Third step:
    sequences analysis

    Physical-chemical

    Molecular Docking


    substrates
    analysis

    CONCLUSIONS
    Before the characterization of the peptide, it was possible to
    identify which regions of the molecule were contributing more
    actively to the nucleo and electrophilic attacks.

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