In the emerging field of systems biology knowledge of protein function is crucial to shaping the understanding of the mechanisms of cellular processes. In theory, molecular function can be assigned by transferring annotations from similar sequences of homologous proteins.

In practice, sequence similarities are so low in distantly related proteins that functionally conserved residues represent a minute portion of the overall sequences and tend to be undetectable with conventional sequence-based approaches. Low sequence similarities in distantly-related proteins are limiting for protein functional annotation, but also negatively impact drug discovery programs.

Structural similarity in proteins thus plays a key role in protein function inference and molecular design. The concept of Most Interacting Residues (MIR) aims at predicting the amino acids more likely to initiate protein folding. An alternative approach describes a protein 3D structure as a series of Tightened End Fragments (TEF). Their spatially close ends have been shown to be mainly located in the folding nucleus.

The resources developed at ASU and TGen in collaboration with various international research laboratories aim at shedding more light on protein structure and folding.

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