I. Callebaut et al., DECIPHERING PROTEIN-SEQUENCE INFORMATION THROUGH HYDROPHOBIC CLUSTER-ANALYSIS (HCA) - CURRENT STATUS AND PERSPECTIVES, Cellular and molecular life sciences, 53(8), 1997, pp. 621-645
Ten years after the idea of hydrophobic cluster analysis (HCA) was con
ceived and first published, theoretical and practical experience has s
hown this unconventional method of protein sequence analysis to be par
ticularly efficient and sensitive, especially with families of sequenc
es sharing low levels of sequence identity. This extreme sensitivity h
as made it possible to predict the functions of genes whose sequence s
imilarities are hardly if at all detectable by current one-dimensional
(1D) methods alone, and offers a new way to explore the enormous amou
nt of data generated by genome sequencing. HCA also provides original
tools to understand fundamental features of protein stability and fold
ing. Since the last review of HCA published in 1990 [1], significant i
mprovements have been made and several new facets have been addressed.
Here we wish to update and summarize this information.