When molecular biologists begin to
investigate a new protein one of the primary questions asked is
what does this protein do? This question partially can be answered
by determining where in the cell it is located. There are many ways
to assess protein location experimentally; however, in 1980 the
researchers Kyte and Doolittle produced an algorithm that assessed
a protein's location using hydropathy based on amino acid sequence.
This method, the Kyte-Doolittle hydropathy plot, has since become
a standard tool in molecular biology.
Using these hydropathy calulations,
we can measure how hydrophobic or hydrophillic a protein is expected
to be in certain regions. If particularly hydrophobic regions exist,
an integral membrane protein is hypothetically indicated. Thus,
a simple computer program can yield potentially important location
information allowing predictions of function.