Protein aggregation is one of the most challenging topics in life sciences,and it is implicated in several human pathologies. The nature and the role of toxic species ishighly debated, with amyloid fibrils being among the most relevant species for theirpeculiar structural and functional properties. Protein dynamics and in particular the abilityto fluctuate through a large number of conformational substates are closely related toprotein function. This Letter focuses on amyloid fibril dynamics, and, to our knowledge, itis the first neutron scattering study on a protein (Concanavalin A) isolated in its fibril state.Our results reveal enhanced atomic fluctuations in amyloid fibrils and indicate that theprotein is “softer” in the fibril state with respect to the native and amorphous aggregatestates. We discuss this finding in terms of a structural interpretation and suggest that theparadigm ordered structure ↔ lower flexibility can be questioned when considering thelocal fast side-chain protein dynamics.
|Numero di pagine||5|
|Rivista||THE JOURNAL OF PHYSICAL CHEMISTRY LETTERS|
|Stato di pubblicazione||Published - 2012|
All Science Journal Classification (ASJC) codes
- Materials Science(all)
- Physical and Theoretical Chemistry