Selected article for: "conformational change and secondary structure"
Author: Courtney Mycroft-West; Dunhao Su; Stefano Elli; Scott Guimond; Gavin Miller; Jeremy Turnbull; Edwin Yates; Marco Guerrini; David Fernig; Marcelo Lima; Mark Skidmore
Title: The 2019 coronavirus (SARS-CoV-2) surface protein (Spike) S1 Receptor Binding Domain undergoes conformational change upon heparin binding
  • Document date: 2020_3_2
    • ID: 0d77ojnb_18
    Snippet: Circular dichroism (CD) spectroscopy detects changes in protein secondary structure that occur in solution using UV radiation. Upon binding, conformational changes are detected and quantified using spectral deconvolution 17 . Indeed, SARS-CoV-2 S1 RBD underwent conformational change in the presence of heparin ( Figure 2) . Combined, Helix content increased by 4.8% and global beta-sheet content decreased by 4.4%. The observed changes further demon.....
    Document: Circular dichroism (CD) spectroscopy detects changes in protein secondary structure that occur in solution using UV radiation. Upon binding, conformational changes are detected and quantified using spectral deconvolution 17 . Indeed, SARS-CoV-2 S1 RBD underwent conformational change in the presence of heparin ( Figure 2) . Combined, Helix content increased by 4.8% and global beta-sheet content decreased by 4.4%. The observed changes further demonstrate that the SARS-CoV-2 S1 RBD interacts with heparin in aqueous solution of physiological significance, whereby the major changes induced by heparin are those associated with antiparallel and helix content.

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