July 2008 issue
Cover illustration: Hydrophobic cores identified from HDX data and depth calculations of the neutron structures of DHFR and endothiapepsin (p. 764). The two DHFR monomers A and B represents the partially occluded and the closed forms, respectively. Proteins are shown in cyan and as cartoon representations. Residues which have backbone amides with depths 3.8 Å are shown as semi-transparent surfaces and with side chains. Exchanged core residues are colored in green whereas non-exchanged core residues are shown in red.