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Structural and Dynamic Characteristics of Intrinsically Disordered Proteins of the SARS-CoV-2 Virus

  • Funded by National Institute of Health Carlos III [El Instituto de Salud Carlos III] (ISCIII)
  • Total publications:0 publications

Grant number: COV20_00764

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Key facts

  • Disease

    COVID-19

  • Funder

    National Institute of Health Carlos III [El Instituto de Salud Carlos III] (ISCIII)

  • Principal Investigator

    Douglas Vinson Laurents, Miguel Mompeán García

  • Research Location

    Spain

  • Lead Research Institution

    Agencia Estatal Consejo Superior de Investigaciones Científicas

  • Research Priority Alignment

    N/A

  • Research Category

    Pathogen: natural history, transmission and diagnostics

  • Research Subcategory

    Pathogen morphology, shedding & natural history

  • Special Interest Tags

    N/A

  • Study Type

    Non-Clinical

  • Clinical Trial Details

    N/A

  • Broad Policy Alignment

    Pending

  • Age Group

    Not Applicable

  • Vulnerable Population

    Not applicable

  • Occupations of Interest

    Not applicable

Abstract

A significant proportion of the SARS-CoV-2 proteome lacks homology to known proteins and appears to have no defined structure. Intrinsically disordered proteins (IDPs) are essential for viral infections as they hijack human regulatory networks. IDPs are refractory to structural analysis by X-ray crystallography or cryoelectron microscopy. The objective of this project is to characterize the partial structure and dynamics of three disordered proteins and three peptides of the SARS-CoV-2 proteome, for example, the segment spanning residues 962-1021: FGATSAALQPEEEQEEDWLDDDSQQTVGQQDGSEDNQTTTIQTIVEVQPQLEMEL TPWQ. We will use NMR spectroscopy and molecular dynamics, which are the only methods that provide information at the atomic level about PIDs.