Glycoprotein molecular dynamics analysis: SARS-CoV-2 spike glycoprotein case study

João Victor Paccini Coutinho, Janaina Macedo-da-Silva, Simon Ngao Mule, Thales Kronenberger, Livia Rosa-Fernandes, Carsten Wrenger, Giuseppe Palmisano*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

2 Citations (Scopus)

Abstract

Molecular Dynamics (MD) is a method used to calculate the movement of atoms and molecules broadly applied to several aspects of science. It involves computational simulation, which makes it, at first glance, not easily accessible. The rise of several automated tools to perform molecular simulations has allowed researchers to navigate through the various steps of MD. This enables to elucidate structural properties of proteins that could not be analyzed otherwise, such as the impact of glycosylation. Glycosylation dictates the physicochemical and biological properties of a protein modulating its solubility, stability, resistance to proteolysis, interaction partners, enzymatic activity, binding and recognition. Given the high conformational and compositional diversity of the glycan chains, assessing their influence on the protein structure is challenging using conventional analytical techniques. In this manuscript, we present a step-by-step workflow to build and perform MD analysis of glycoproteins focusing on the SPIKE glycoprotein of SARS-CoV-2 to appraise the impact of glycans in structure stabilization and antibody occlusion.

Original languageEnglish
Title of host publicationProtein interaction networks
EditorsRossen Donev
Place of PublicationUnited States
PublisherElsevier Academic Press
Chapter9
Pages277-309
Number of pages33
ISBN (Print)9780323992312
DOIs
Publication statusPublished - 2022

Publication series

NameAdvances in Protein Chemistry and Structural Biology
Volume131
ISSN (Print)1876-1623
ISSN (Electronic)1876-1631

Keywords

  • Antibody accessibility
  • Antigen-antibody interaction
  • Glycans
  • Glycoproteins
  • Molecular dynamics simulation
  • Protein structure
  • SARS-CoV-2
  • Solvent accessibility

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