Mixture distributions are extensively used as a modeling tool in diverse areas from machine learning to communications engineering to physics, and obtaining bounds on the entropy of mixture distributions is of fundamental importance in many of these applications. This article provides sharp bounds on the entropy concavity deficit, which is the difference between the differential entropy of the mixture and the weighted sum of differential entropies of constituent components. Toward establishing lower and upper bounds on the concavity deficit, results that are of importance in their own right are obtained. In order to obtain nontrivial upper bounds, properties of the skew-divergence are developed and notions of “skew”$f$-divergences are introduced; a reverse Pinsker inequality and a bound on Jensen-Shannon divergence are obtained along the way. Complementary lower bounds are derived with special attention paid to the case that corresponds to independent summation of a continuous and a discrete random variable. Several applications of the bounds are delineated, including to mutual information of additive noise channels, thermodynamics of computation, and functional inequalities.

Motivated by the entropy computations relevant to the evaluation of decrease in entropy in bit reset operations, the authors investigate the deficit in an entropic inequality involving two independent random variables, one continuous and the other discrete. In the case where the continuous random variable is Gaussian, we derive strong quantitative bounds on the deficit in the inequality. More explicitly it is shown that the decay of the deficit is sub-Gaussian with respect to the reciprocal of the standard deviation of the Gaussian variable. What is more, up to rational terms these results are shown to be sharp.

Intracellular transport is an essential function in eucaryotic cells, facilitated by motor proteins-proteins converting chemical energy into kinetic energy. It is understood that motor proteins work in teams enabling unidirectional and bidirectional transport of intracellular cargo over long distances. Disruptions of the underlying transport mechanisms, often caused by mutations that alter single motor characteristics, are known to cause neurodegenerative diseases. For example, phosphorylation of kinesin motor domain at the serine residue is implicated in Huntington's disease, with a recent study of phosphorylated and phosphomimetic serine residues indicating lowered single motor stalling forces. In this article we report the effects of mutations of this nature on transport properties of cargo carried by multiple wild-type and mutant motors. Results indicate that mutants with altered stall forces might determine the average velocity and run-length even when they are outnumbered by wild type motors in the ensemble. It is shown that mutants gain a competitive advantage and lead to an increase in the expected run-length when the load on the cargo is in the vicinity of the mutant's stalling force or a multiple of its stalling force. A separate contribution of this article is the development of a semi-analytic method to analyze transport of cargo by multiple motors of multiple types. The technique determines transition rates between various relative configurations of motors carrying the cargo using the transition rates between various absolute configurations. This enables a computation of biologically relevant quantities like average velocity and run-length without resorting to Monte Carlo simulations. It can also be used to introduce alterations of various single motor parameters to model a mutation and to deduce effects of such alterations on the transport of a common cargo by multiple motors. Our method is easily implementable and we provide a software package for general use.