Evaluation of the Multilook Size in Polarimetric Optimization of Differential SAR Interferograms

The interferometric coherence is a measure of the correlation between two SAR images and constitutes a commonly used estimator of the phase quality. Its estimation requires a spatial average within a 2-D window, usually named as multilook. The multilook processing allows reducing noise at the expenses of a resolution loss. In this letter, we analyze the influence of the multilook size while applying a polarimetric optimization of the coherence. The same optimization algorithm has been carried out with different multilook sizes and also with the nonlocal SAR filter filter, which has the advantage of preserving the original resolution of the interferogram. Our experiments have been carried out with a single pair of quad-polarimetric RADARSAT-2 images mapping the Mount Etna's volcanic eruption of May 2008. Results obtained with this particular data set show that the coherence is increased notably with respect to conventional channels when small multilook sizes are employed, especially over low-vegetated areas. Conversely, very decorrelated areas benefit from larger multilook sizes but do not exhibit an additional improvement with the polarimetric optimization

Binding Free Energy Landscape of Domain-Peptide Interactions

Peptide recognition domains (PRDs) are ubiquitous protein domains which mediate large numbers of protein interactions in the cell. How these PRDs are able to recognize peptide sequences in a rapid and specific manner is incompletely understood. We explore the peptide binding process of PDZ domains, a large PRD family, from an equilibrium perspective using an all-atom Monte Carlo (MC) approach. Our focus is two different PDZ domains representing two major PDZ classes, I and II. For both domains, a binding free energy surface with a strong bias toward the native bound state is found. Moreover, both domains exhibit a binding process in which the peptides are mostly either bound at the PDZ binding pocket or else interact little with the domain surface. Consistent with this, various binding observables show a temperature dependence well described by a simple two-state model. We also find important differences in the details between the two domains. While both domains exhibit well-defined binding free energy barriers, the class I barrier is significantly weaker than the one for class II. To probe this issue further, we apply our method to a PDZ domain with dual specificity for class I and II peptides, and find an analogous difference in their binding free energy barriers. Lastly, we perform a large number of fixed-temperature MC kinetics trajectories under binding conditions. These trajectories reveal significantly slower binding dynamics for the class II domain relative to class I. Our combined results are consistent with a binding mechanism in which the peptide C terminal residue binds in an initial, rate-limiting step