A new model of proteins seeks to
explain how enzymes extract energy form their vicinity and put it to
use in regulating cell chemistry. Enzymes are huge protein
molecules that play a crucial role in catalyzing chemical reactions
among other molecules or atoms by lowering the energy barrier that
would otherwise keep the reaction from happening. Enzymes can
therefore be considered as energy-processing
chemical-reaction-facilitating machines.
They are usually large,
typically containing thousands of heavy (non-hydrogen) atoms, but of
these only a few dozen atoms actually participate in the catalytic
process. Addressing this important issue, a team of scientists at
the Ecole Normale Superieure (Lyon, France) and the Ecole
Polytechnique Federale de Lausanne (Switzerland) have concentrated
on modeling the behavior of the stiff parts of the enzyme since they
believe that some of the energy used in carrying out the catalytic
task is stored not just as chemical energy (in the form of adenosine
triphosphate, or ATP, the all-purpose “food” of cells) but also as
mechanical energy in the form of a waggling or “breathing” motion in
the stiffer parts of the enzyme.
Extending this research to
proteins in general, Yves-Henri Sanejouand
(yves-henri.sanejouand@ens-lyon.fr, 33-04-72-72-8870) says that he
and his colleagues would like to scrutinize in more detail the
nonlinear process by which some proteins catch and store thermal
energy from their environment and also how chemical energy can be
turned into mechanical energy, such as in muscle contraction.
(Juanico et al., Physical Review Letters, upcoming article)