The conformational properties of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) within proteins are of considerable interest. Despite their inability to fold spontaneously as autonomous units (Dunker et al. 2001; Dyson 2011; Gsponer and Babu 2009; Tompa 2012; Uversky 2002, 2011) IDPs and IDRs play important functional roles in biology (Dunker 2007; Dunker et al. 2008; Dyson and Wright 2005; Forman-Kay and Mittag 2013; Liu, Faeder, and Camacho 2009; Romero, Obradovic, and Dunker 2004; Xie et al. 2007). IDPs and IDRs play prominent roles in cell signaling and transcription regulation and they serve as hubs in protein interaction networks (Dunker et al. 2005; Haynes et al. 2006; Singh, Ganapathi, and Dash 2007). Mutations within IDPs/IDRs are implicated in several diseases (Babu et al. 2011; Uversky, Oldfield, and Dunker 2008; Uversky et al. 2009).
|Title of host publication||Computational Approaches to Protein Dynamics|
|Subtitle of host publication||From Quantum to Coarse-Grained Methods|
|Number of pages||23|
|State||Published - Jan 1 2014|