Abriata, Luciano A.Dal Peraro, Matteo2020-06-182020-06-182020-06-182020-05-2610.1021/acs.jcim.0c00177https://infoscience.epfl.ch/handle/20.500.14299/169396WOS:000537653400008Protein dynamics is undoubtedly a pervasive ingredient in all biological functions. However, structural biology has been strongly driven by a static-centered view of protein architecture. We argue that the recent advances of cryo-electron microscopy (EM) have the potential to more broadly explore the conformational landscapes of protein complexes and therefore will enhance our ability to predict the diverse conformations of tertiary and quaternary protein structures that are functionally relevant in physiological conditions.Chemistry, MedicinalChemistry, MultidisciplinaryComputer Science, Information SystemsComputer Science, Interdisciplinary ApplicationsPharmacology & PharmacyChemistryComputer Sciencecontact predictionscoevolutiondynamicsensemblesequencetext::journal::journal article::research article