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Study of SARS-CoV-2 Spike Protein by Surface Enhanced Raman Spectroscopy and Transmission Electron Microscopy
ref [20] · 2501.17212 · notice #9415 · dispute
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A. C. Walls, Y. J. Park, M. A. Tortorici, A. Wall, A. T. McGuire, D. Veesler, Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein, Cell. 180 (2020) 281- 292, https://doi.org/10.1016/j.cell.2020.02.058. 15 Supporting Information Study of SARS-CoV-2 Spike Protein by Surface Enhanced Raman Spectroscopy and Transmission Electron Microscopy Monika Ghalawat2, Virendra Kumar Meena1, Sharda Prasad1, Pankaj Poddar2#, Atanu Basu1* 1 ICMR-National Institute of Virology, 20A Ambedkar Road Pune, India 2 CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road Pune, India #,* Joint corresponding authors Corresponding Author E-mail: p.poddar@ncl.res.in#, basu.atanu@gov.in* Figure S1. The sequence of SARS-CoV-2 full-length spike protein from protein accession database code YP-009724390.1. The tyrosine (Tyr; Y), tryptophan (Trp; W), and phenylalanine (Phe; F) amino acids at distinct positions are highlighted by pink, blue and yellow, respectively. [Ref. https://www.ncbi.nlm.nih.gov/protein/YP_009724390.1] 1 MFVFLVLLPLVSSQCVNLTT RTQLPPAYTN SFTRGVYYPD KVFRSSVLHS TQDLFLPFFS 61 NVTWFHAIHV SGTNGTKRFD NPVLPFNDGV YFASTEKSNI IRGWIFGTTL DSKTQSLLIV 121 NNATNVVIKV CEFQFCNDPF LGVYYHKNNK SW