Genome sequencing projects are revealing a large number of biologically
important proteins having the tandem arrays of up to 40 residue repeats. These
proteins are under-represented
in the structural databases because their large molecular weight and the
elongated shapes hamper X-ray crystallography and NMR studies. The difficulties
of the experimental studies increase importance of the bioinformatics approaches.
We pioneered bioinformatics analysis, classification, structural prediction and
modelling of proteins with repeats which fold into solenoid-like arrangement.
Further development of reliable methods for identifications of the repetitive
protein motifs (see our library of sequence profiles) and ab initio prediction of their 3D structures promise to be fertile
research subjects of structural bioinformatics.
Over the last years a number of evidences have been accumulated about the high incidence of tandem repeats in the amino acid sequences of virulence factors of pathogens and some amyloids and prions. Thus, discovery and structure-function predictions of these domains may lead to the identification of targets for new antibiotics and vaccines against emerging infectious diseases and to the development of inhibitors of amyloidogenesis.