Laboratory of Cell Physiology, Institute of Cytology, Russian Academy
of Sciences, Tikhoretsky Ave 4, St, Petersburg 194064, Russia.
Abstract
According to the hypothesis explored in this paper, native aggregation
is genetically controlled (programmed) reversible aggregation that
occurs when interacting proteins form new temporary structures through
highly specific interactions. It is assumed that Anfinsen's dogma may
be extended to protein aggregation: composition and amino acid
sequence determine not only the secondary and tertiary structure of
single protein, but also the structure of protein aggregates
(associates). Cell function is considered as a transition between two
states (two states model), the resting state and state of activity
(this applies to the cell as a whole and to its individual
structures). In the resting state, the key proteins are found in the
following inactive forms: natively unfolded and globular. When the
cell is activated, secondary structures appear in natively unfolded
proteins (including unfolded regions in other proteins), and globular
proteins begin to melt and their secondary structures become available
for interaction with the secondary structures of other proteins. These
temporary secondary structures provide a means for highly specific
interactions between proteins. As a result, native aggregation creates
temporary structures necessary for cell activity. "One of the
principal objects of theoretical research in any department of
knowledge is to find the point of view from which the subject appears
in its greatest simplicity."Josiah Willard Gibbs (1839-1903).
Full text: http://vladimirmatveev.ru