Abstract
Molecular chaperones are a wide group of unrelated protein families
whose role is to assist others proteins. Comparably, under environmental
stress, stress proteins behave as biocatalysts of protein stabilization. Stress
proteins include a large class of proteins that were originally termed heat
shock proteins (HSPs) due to their initial discovery in tissues exposed to
elevated temperatures. Many, but not all, stress proteins and HSPs are
molecular chaperones. Moreover, not all HSPs are derivable from stress. HSPs
are structurally diversified by the contribution of various domains having
specific roles. HSPs have been grouped, mainly on the basis of their molecular
masses, into specific families that include small HSPs
(sHSPs)/α-crystallins, HSP10s, HSP40s, HSP60s, HSP70s,
HSP90s, HSP100s and HSP110s. The names of these major families are historical
artefacts with limited information content. Using the current databases, names
and proteic domains of many molecular chaperones in different species were
analyzed. Although traditional names of HSPs are trivial, it is unrealistic to
suggest replacing them, because they are preferred and widely used. Here we
suggest that these traditional names be chaperoned, in silico, by a
systematic nomenclature. Thus, for example, with the same intent of use of
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