AUTHOR=Khan Faez Iqbal , Lobb Kevin A. , Lai Dakun 

TITLE=The Molecular Basis of the Effect of Temperature on the Structure and Function of SARS-CoV-2 Spike Protein

JOURNAL=Frontiers in Molecular Biosciences

VOLUME=Volume 9 - 2022

YEAR=2022

URL=https://www.frontiersin.org/journals/molecular-biosciences/articles/10.3389/fmolb.2022.794960

DOI=10.3389/fmolb.2022.794960

ISSN=2296-889X

ABSTRACT=The remarkable rise of the current COVID-19 pandemic to every part of the globe has lifted the key concerns for the current public health care system. The spike (S) protein of SARS-CoV-2 shows an important part in the cell membrane fusion and receptor recognition. It is a key target for vaccine production. Several researchers studied the nature of this protein under various environmental conditions. In this work, we applied molecular modeling and extensive molecular dynamics simulations approaches at 0℃ (273.15K), 20℃ (293.15K), 40℃ (313.15K), and 60℃ (333.15K) to study the detailed conformational alterations in SARS-CoV-2 S protein. Our aim is to understand the influence of temperatures on the structure, function and dynamics of the S protein of SARS-CoV-2. The structural deviations, atomic and residual fluctuations were least at low (0℃) and high (60℃) temperature. Even the internal residues of SARS-CoV-2 S protein are not accessible to solvent at high temperature. Further, there was no unfolding of SARS-CoV-2 spike S reported at higher temperature. The most stable conformations of SARS-CoV-2 S protein was reported at 20℃, but the free energy minimum region of SARS-CoV-2 S protein was sharper at 40℃ than other temperatures. Our findings revealed that higher temperatures have little or no influence on the stability and folding of SARS-CoV-2 S protein.