Callebaut, I, Labesse, G, P Durand, Poupon, A, Canard, L, Chomilier, J, Henrissat, B and Mornon, JP (1997), "Deciphering protein sequence information through hydrophobic cluster analysis (HCA): current status and perspectives.", Cell Mol Life Sci, 53, 8: 621-45.
Abstract: Ten years after the idea of hydrophobic cluster analysis (HCA) was
conceived and first published, theoretical and practical experience has
shown this unconventional method of protein sequence analysis to be
particularly efficient and sensitive, especially with families of sequences
sharing low levels of sequence identity. This extreme sensitivity has
made it possible to predict the functions of genes whose sequence
similarities are hardly if at all detectable by current one-dimensional
(1D) methods alone, and offers a new way to explore the enormous
amount of data generated by genome sequencing. HCA also provides
original tools to understand fundamental features of protein stability
and folding. Since the last review of HCA published in 1990 [1],
significant improvements have been made and several new facets have been
addressed. Here we wish to update and summarize this information.
