title: Extended disordered proteins: targeting function with less scaffold.
abstract: It has been estimated that a large fraction of cellular proteins are natively disordered. Current opinion largely holds that natively disordered proteins are more 'adaptive', leading to advantages in regulation and in binding diverse ligands. Here, we argue for another, simple, physically based reason. Disordered proteins often have large intermolecular interfaces, the size of which is dictated by protein function. For proteins to be stable as monomers with extensive interfaces, protein size would need to be 2-3 times larger. This would either increase cellular crowding or enlarge the size of the cell by 15-30%, owing to the increase in the sequence length. Smaller sizes of cells, proteins, DNA and RNA conserve energy. Thus, disordered proteins provide a simple yet elegant solution to having large intermolecular interfaces, but with smaller protein, genome and cell sizes.
authors.affiliation: Laboratory of Experimental and Computational Biology, NCI- Frederick, MD 21702, USA.
authors.forename: Kannan
authors.initials: K
authors.lastname: Gunasekaran
authors.forename: Chung-Jung
authors.initials: CJ
authors.lastname: Tsai
authors.forename: Sandeep
authors.initials: S
authors.lastname: Kumar
authors.forename: David
authors.initials: D
authors.lastname: Zanuy
authors.forename: Ruth
authors.initials: R
authors.lastname: Nussinov
mesh_terms: D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013329:Structure-Activity Relationship; D013499:Surface Properties; D013816:Thermodynamics
chemical_list: D011506:Proteins