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dc.contributor.authorBemporad, Francesco
dc.date.accessioned2022-05-31T10:15:21Z
dc.date.available2022-05-31T10:15:21Z
dc.date.issued2009
dc.identifierONIX_20220531_9788884539465_149
dc.identifier.issn2612-8020
dc.identifier.urihttps://library.oapen.org/handle/20.500.12657/54865
dc.description.abstractFolding and misfolding of proteins are considered two sides of the same coin. The delicate equilibrium existing between these two processes is crucial for any living organism and its alterations can lead to the onset of several tremendous diseases, such as Alzheimer's and Parkinson's disease. The attainment of a profound knowledge of folding/misfolding processes is a key step to understand how life works and for discovering new therapies to these diseases. In this work the author shows that proteins can display enzymatic activity even in the absence of a compact three-dimensional structure, with important implications for the study of protein enzymes. Furthermore, the author investigates the formation of protein aggregates similar to those observed in patients of amyloid-related diseases.
dc.languageEnglish
dc.relation.ispartofseriesPremio Tesi di Dottorato
dc.subject.otherMedicina
dc.subject.otherBiologia
dc.subject.otherChimica
dc.titleFolding and aggregation studies in the acylphosphatase-like family
dc.typebook
oapen.identifier.doi10.36253/978-88-8453-946-5
oapen.relation.isPublishedBybf65d21a-78e5-4ba2-983a-dbfa90962870
oapen.relation.isbn9788884539465
oapen.relation.isbn9788884539458
oapen.relation.isbn9788892737686
oapen.series.number6
oapen.pages126
oapen.place.publicationFirenze


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