Folding 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.
University of Florence, Italy - ORCID: 0000-0002-0643-6249
Titolo del libro
Folding and aggregation studies in the acylphosphatase-like family
Autori
Francesco Bemporad
Opera sottoposta a peer review
Numero di pagine
126
Anno di pubblicazione
2009
Copyright
© 2009 Author(s)
Licenza d'uso
Licenza dei metadati
Editore
Firenze University Press
DOI
10.36253/978-88-8453-946-5
ISBN Print
978-88-8453-945-8
eISBN (pdf)
978-88-8453-946-5
eISBN (xml)
978-88-9273-768-6
Collana
Premio Tesi di Dottorato
ISSN della collana
2612-8039
e-ISSN della collana
2612-8020