  The high accuracy exhibited by biological information transcription processes
is due to kinetic proofreading, i.e., by a mechanism which reduces the error
rate of the information-handling process by driving it out of equilibrium. We
provide a consistent thermodynamic description of enzyme-assisted assembly
processes involving competing substrates, in a Master Equation framework. We
introduce and evaluate a measure of the efficiency based on rigorous
non-equilibrium inequalities. The performance of several proofreading models
are thus analyzed and the related time, dissipation and efficiency vs. error
trade-offs exhibited for different discrimination regimes. We finally introduce
and analyze in the same framework a simple model which takes into account
correlations between consecutive enzyme-assisted assembly steps. This work
highlights the relevance of the distinction between energetic and kinetic
discrimination regimes in enzyme-substrate interactions.
