Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.3389/fmolb.2022.794960 http://scihub22266oqcxt.onion/10.3389/fmolb.2022.794960 35463957!9019816!35463957     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Front+Mol+Biosci 2022 ; 9 (ä): 794960 Nephropedia Template TP {{tp|p=35463957|t=2022. The Molecular Basis of the Effect of Temperature on the Structure and Function of SARS-CoV-2 Spike Protein |pdf=|usr=}}{{35463957}} gab.com Text The Molecular Basis of the Effect of Temperature on the Structure and Function of SARS-CoV-2 Spike Protein JO: Front Mol Biosci http://www.kidney.de/pget.php?&tw=1&pmid=35463957 #FOAvip The remarkable rise of the current COVID-19 pandemic to every part of the globe has raised key concerns for the current public healthcare 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 simulation approaches at 0 degrees C (273.15 K), 20 degrees C (293.15 K), 40 degrees C (313.15 K), and 60 degrees C (333.15 K) to study the detailed conformational alterations in the 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, and atomic and residual fluctuations were least at low (0 degrees C) and high (60 degrees C) temperature. Even the internal residues of the SARS-CoV-2 S protein are not accessible to solvent at high temperature. Furthermore, there was no unfolding of SARS-CoV-2 spike S reported at higher temperature. The most stable conformations of the SARS-CoV-2 S protein were reported at 20 degrees C, but the free energy minimum region of the SARS-CoV-2 S protein was sharper at 40 degrees C than other temperatures. Our findings revealed that higher temperatures have little or no influence on the stability and folding of the SARS-CoV-2 S protein. Twit Text FOAVip The Molecular Basis of the Effect of Temperature on the Structure and Function of SARS-CoV-2 Spike Protein ????Front Mol Biosci http://www.kidney.de/pget.php?&tw=1&pmid=35463957 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35463957 #FOAvip English Wikipedia <ref>{{Cite pmid|35463957}}</ref> The Molecular Basis of the Effect of Temperature on the Structure and Function of SARS-CoV-2 Spike Protein #MMPMID35463957 Khan FI; Lobb KA; Lai D Front Mol Biosci 2022[]; 9 (ä): 794960 PMID35463957show ga The remarkable rise of the current COVID-19 pandemic to every part of the globe has raised key concerns for the current public healthcare 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 simulation approaches at 0 degrees C (273.15 K), 20 degrees C (293.15 K), 40 degrees C (313.15 K), and 60 degrees C (333.15 K) to study the detailed conformational alterations in the 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, and atomic and residual fluctuations were least at low (0 degrees C) and high (60 degrees C) temperature. Even the internal residues of the SARS-CoV-2 S protein are not accessible to solvent at high temperature. Furthermore, there was no unfolding of SARS-CoV-2 spike S reported at higher temperature. The most stable conformations of the SARS-CoV-2 S protein were reported at 20 degrees C, but the free energy minimum region of the SARS-CoV-2 S protein was sharper at 40 degrees C than other temperatures. Our findings revealed that higher temperatures have little or no influence on the stability and folding of the SARS-CoV-2 S protein. äThe Molecular Basis of the Effect of Temperature on the Structure and (epmc).pdf DeepDyve Pubget Overpricing