https://www.socictopen.socict.org/files/original/f9154d62d7def44646f32f19c42d0d1d.pdf 1d471687397e4e4c437960aabd190d54 Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Coronavirus Description An account of the resource Dominio científico: Coronavirus Text A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text. Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource The dimer-monomer equilibrium of SARS-CoV-2 main protease is affected by small molecule inhibitors Creator An entity primarily responsible for making the resource Lucia Silvestrini, Norhan Belhaj, Lucia Comez, Yuri Gerelli, Antonino Lauria, Valeria Libera, Paolo Mariani, Paola Marzullo, Maria Grazia Ortore, Antonio Palumbo Piccionello, Caterina Petrillo, Lucrezia Savini, Alessandro Paciaroni, Francesco Spinozzi Description An account of the resource Abstract The maturation of coronavirus SARS-CoV-2, which is the etiological agent at the origin of the COVID-19 pandemic, requires a main protease Mpro to cleave the virus-encoded polyproteins. Despite a wealth of experimental information already available, there is wide disagreement about the Mpro monomer-dimer equilibrium dissociation constant. Since the functional unit of Mpro is a homodimer, the detailed knowledge of the thermodynamics of this equilibrium is a key piece of information for possible therapeutic intervention, with small molecules interfering with dimerization being potential broad-spectrum antiviral drug leads. In the present study, we exploit Small Angle X-ray Scattering (SAXS) to investigate the structural features of SARS-CoV-2 Mpro in solution as a function of protein concentration and temperature. A detailed thermodynamic picture of the monomer-dimer equilibrium is derived, together with the temperature-dependent value of the dissociation constant. SAXS is also used to study how the Mpro dissociation process is affected by small inhibitors selected by virtual screening. We find that these inhibitors affect dimerization and enzymatic activity to a different extent and sometimes in an opposite way, likely due to the different molecular mechanisms underlying the two processes. The Mpro residues that emerge as key to optimize both dissociation and enzymatic activity inhibition are discussed. Date A point or period of time associated with an event in the lifecycle of the resource 2021 Identifier An unambiguous reference to the resource within a given context 10.1038/s41598-021-88630-9 Source A related resource from which the described resource is derived Epidemiology and Health Publisher An entity responsible for making the resource available Korean Society of Epidemiology Coverage The spatial or temporal topic of the resource, the spatial applicability of the resource, or the jurisdiction under which the resource is relevant Science, Medicine