In this chapter, we describe an experimental approach based on the single - molecule force spectroscopy (SMFS) technique that can be employed to gain insights on the conformational equilibria of monomeric intrinsically disordered proteins (IDPs). We report how this approach was utilized for characterizing the conformational diversity of a - synuclein, a Parkinson - involved IDP. We also offer a brief introduction to the SMFS technique, a description of the various SMFS experimental approaches that were applied to protein folding studies, and a summary of the available SMFS studies on IDPs or disordered segments. Finally, we propose plausible SMFS research perspectives that could be helpful in gaining further knowledge on the fascinating subject of IDPs. © 2010 John Wiley and Sons, Inc.
Monitoring the Conformational Equilibria of Monomeric Intrinsically Disordered Proteins by Single-Molecule Force Spectroscopy
Brucale Marco;
2010
Abstract
In this chapter, we describe an experimental approach based on the single - molecule force spectroscopy (SMFS) technique that can be employed to gain insights on the conformational equilibria of monomeric intrinsically disordered proteins (IDPs). We report how this approach was utilized for characterizing the conformational diversity of a - synuclein, a Parkinson - involved IDP. We also offer a brief introduction to the SMFS technique, a description of the various SMFS experimental approaches that were applied to protein folding studies, and a summary of the available SMFS studies on IDPs or disordered segments. Finally, we propose plausible SMFS research perspectives that could be helpful in gaining further knowledge on the fascinating subject of IDPs. © 2010 John Wiley and Sons, Inc.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
