Cover illustration The informativeness of protein flexibility derived from molecular simulations was investigated by analyzing its ability in detecting similarities among a large set of distant homologous proteins. In particular, the detailed analysis of the d.16 fold (FAD-linked reductases, C terminal domain) confirmed that, when the biologically relevant dynamics is embedded in the domain, the 'flexibility code' is conserved in the family. Here the monoamine oxidase B structure is showed to highlight the characteristics of this fold (colored according to secondary structures) that faces the active site and the FAD cofactor (in green). For further details see Pandini et al. pp. 285-299
[Table of Contents]