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10.1021/acs.jpcb.2c01272 http://scihub22266oqcxt.onion/10.1021/acs.jpcb.2c01272 35477296!ä!35477296 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Phys+Chem+B 2022 ; 126 (18): 3425-3430 Nephropedia Template TP {{tp|p=35477296|t=2022. Structure and Orientation of the SARS-Coronavirus-2 Spike Protein at Air-Water Interfaces |pdf=|usr=}}{{35477296}} gab.com Text Structure and Orientation of the SARS-Coronavirus-2 Spike Protein at Air-Water Interfaces JO: J Phys Chem B http://www.kidney.de/pget.php?&tw=1&pmid=35477296 #FOAvip The SARS coronavirus 2 (SARS-CoV-2) spike protein is located at the outermost perimeter of the viral envelope and is the first component of the virus to make contact with surrounding interfaces. The stability of the spike protein when in contact with surfaces plays a deciding role for infection pathways and for the viability of the virus after surface contact. While cryo-EM structures of the spike protein have been solved with high resolution and structural studies in solution have provided information about the secondary and tertiary structures, only little is known about the folding when adsorbed to surfaces. We here report on the secondary structure and orientation of the S1 segment of the spike protein, which is often used as a model protein for in vitro studies of SARS-CoV-2, at the air-water interface using surface-sensitive vibrational sum-frequency generation (SFG) spectroscopy. The air-water interface plays an important role for SARS-CoV-2 when suspended in aerosol droplets, and it serves as a model system for hydrophobic surfaces in general. The SFG experiments show that the S1 segment of the spike protein remains folded at the air-water interface and predominantly binds in its monomeric state, while the combination of small-angle X-ray scattering and two-dimensional infrared spectroscopy measurements indicate that it forms hexamers with the same secondary structure in aqueous solution. Twit Text FOAVip Structure and Orientation of the SARS-Coronavirus-2 Spike Protein at Air-Water Interfaces ????J Phys Chem B http://www.kidney.de/pget.php?&tw=1&pmid=35477296 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35477296 #FOAvip English Wikipedia <ref>{{Cite pmid|35477296}}</ref> Structure and Orientation of the SARS-Coronavirus-2 Spike Protein at Air-Water Interfaces #MMPMID35477296 Bregnhoj M; Roeters SJ; Chatterley AS; Madzharova F; Mertig R; Pedersen JS; Weidner T J Phys Chem B 2022[May]; 126 (18): 3425-3430 PMID35477296show ga The SARS coronavirus 2 (SARS-CoV-2) spike protein is located at the outermost perimeter of the viral envelope and is the first component of the virus to make contact with surrounding interfaces. The stability of the spike protein when in contact with surfaces plays a deciding role for infection pathways and for the viability of the virus after surface contact. While cryo-EM structures of the spike protein have been solved with high resolution and structural studies in solution have provided information about the secondary and tertiary structures, only little is known about the folding when adsorbed to surfaces. We here report on the secondary structure and orientation of the S1 segment of the spike protein, which is often used as a model protein for in vitro studies of SARS-CoV-2, at the air-water interface using surface-sensitive vibrational sum-frequency generation (SFG) spectroscopy. The air-water interface plays an important role for SARS-CoV-2 when suspended in aerosol droplets, and it serves as a model system for hydrophobic surfaces in general. The SFG experiments show that the S1 segment of the spike protein remains folded at the air-water interface and predominantly binds in its monomeric state, while the combination of small-angle X-ray scattering and two-dimensional infrared spectroscopy measurements indicate that it forms hexamers with the same secondary structure in aqueous solution. |*COVID-19[MESH] |*SARS-CoV-2[MESH] |Humans[MESH] |Spike Glycoprotein, Coronavirus/chemistry[MESH]Structure and Orientation of the SARS-Coronavirus-2 Spike Protein at A(epmc).pdf DeepDyve Pubget Overpricing