Hinge residues tend to be on the surface, since steric clashes would often prevent them from being in the core

<p><b>Copyright information:</b></p><p>Taken from "Hinge Atlas: relating protein sequence to sites of structural flexibility"</p><p>http://www.biomedcentral.com/1471-2105/8/167</p><p>BMC Bioinformatics 2007;8():167-167.</p><p>Published online 22 May 2007</p><p>PMCID:PMC1913541.</p><p></p> We computed the solvent accessible surface area for the backbone atoms of all residues in the Hinge Atlas and binned the residues by this quantity. Bin #1 contains the 20% of all residues with the largest solvent accessible surface area, and bin #5 contains the 20% of residues with the smallest solvent accessible surface area. The first two bins (together representing the 40% of residues with highest surface area) are enriched with hinges in a highly significant manner. Conversely, the last two bins (lowest 40% ASA) are significantly low in hinges