Figure 1. One disordered protein, two partners. The regions of the extreme C-terminal sequence of p53 (SwissProt ID P53_HUMAN) that bind to both Cyclin A2 (green bar) and to S100 (red bar) are shown. Also shown are renderings of the corresponding experimental determined complexes, where molecular surfaces of cyclin A2 (blue) and S100 (orange) are shown bound to ribbon representations of p53 (green and red, respectively). Structures were rendered from the PDB entries 1DT7 for Cylcin A2 and 1H26 for S100. This figure was prepared by Christopher J. Oldfield from his PhD Thesis research.

Figure 2. Two disordered proteins, one partner. Shown are the chemical structures of representatives of two 14-3-3 binding motifs m1 and m2, which are R-(S/Ar)-[+]-pS-[LEAM]-P and R-X-[Y/F]-[+]-pS-[LEAM]-P, respectively. The chemical structures represent the bonds made between the binding peptides and 14-3-3, as well as solvent, where hydrophobic interactions are represented by proximity and hydrogen bonds are represented by red dashed lines. 14-3-3 residues are shown in green, crystallographic water molecules in blue and implied water molecules (i.e. exposed donors or acceptors without observed hydrogen bonds) in red. Hydrogen bonds were calculated for the m1 and m2 structures from the PDB entries 1QJB and 1QJA, respectively. This figure was prepared by Christopher J. Oldfield from his PhD Thesis research.

Figure 3. Amino acid profile for disordered proteins. (a) Composition of ordered proteins (CO), (b) composition of disordered proteins (CD), (c) relative composition of disordered proteins relative to ordered proteins, i.e. (CD–CO)/CO. Ordered proteins were taken compiled from all monomeric proteins in the Protein Quaternary Structure server (http://pqs.ebi.ac.uk) without bound ligands and clustered at 25% sequence identity, which consists of 1160 proteins with 294 297 residues with defined electron density. Disordered proteins and regions were taken from DisProt release 3.5. Amino acids are arranged from left to right in terms of increasing flexibility, where this term is estimated from amino acid residue average B-factor values. This figure was prepared by Christopher J. Oldfield from his PhD Thesis research.

Figure 4. Intrinsic disorder, protein function and alternative splicing. Binding regions for a given molecule are indicated by the corresponding colour bar(s) along the representation of full length BRCA1. BRCA1 is represented by bars where blue regions have been experimentally determined to be ordered and red regions have been experimentally determined to be disordered. Regions removed from splice variants of full-length BRCA1 are indicated by dotted lines. Partner binding regions and phosphorylation sites were gathered from the literature and from the SwissProt database, and alternatively spliced variants were taken from the representative splicing variants from the Alternative Splicing Gallery. This figure was prepared by Christopher J. Oldfield from his PhD Thesis research.