About the image
A ribbon representation of the protein crambin (PDB code 1CRN), one of several small proteins which have been widely used in experimental studies of protein folding.

Dr. Jacobs has long been a fan of the so-called "threading" methods and related sequence-structure matching methods. These methods "fit" a protein sequence onto a (template of a) protein structure. By fitting a protein sequence with no known structural data onto (template(s) of) the structures found in the Protein Data Bank (PDB), scientists can obtain a low resolution model structure for that protein. Using this structural model one can better interpret mutational data, search for potential substrate binding sites and make more accurate comparisons of the protein of interest with other related proteins.

These sequence-to-structure matching methods are the linch-pin of the structural genome projects. The structural genome projects aim to obtain an atomic structure of a representative of every protein family. Using these representative structures, one can then map all sequences of the protein family onto the fold of the known structures and thus obtain approximate structural models for all protein sequences. The structural genome project approach effectively by-passes the need to solve the protein folding problem or to determine the atomic structure of all proteins.