title: Energetic and topological determinants of a phosphorylation-induced disorder-to-order protein conformational switch.
abstract: We show that the phosphorylation of 4E-BP2 acts as a triggering event to shape its folding-function landscape that is delicately balanced between conflicting favorable energetics and intrinsically unfavorable topological connectivity. We further provide first evidence that the fitness landscapes of proteins at the threshold of disorder can differ considerably from ordered domains.
authors.affiliation: Department of Biotechnology, Bhupat & Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai 600036, India. athi@iitm.ac.in.
authors.forename: Soundhararajan
authors.initials: S
authors.lastname: Gopi
authors.forename: Nandakumar
authors.initials: N
authors.lastname: Rajasekaran
authors.forename: Animesh
authors.initials: A
authors.lastname: Singh
authors.forename: Sayan
authors.initials: S
authors.lastname: Ranu
authors.forename: Athi N
authors.initials: AN
authors.lastname: Naganathan
mesh_terms: D039642:Eukaryotic Initiation Factors / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation; D011487:Protein Conformation; D017510:Protein Folding; D013816:Thermodynamics
chemical_list: C104151:EIF4EBP2 protein, human; D039642:Eukaryotic Initiation Factors