The effect of low solubility organic acids on the hygroscopicity of sodium halide aerosols

In order to accurately assess the influence of fatty acids on the hygroscopic and other physicochemical properties of sea salt aerosols, hexanoic, octanoic or lauric acid together with sodium halide salts (NaCl, NaBr and NaI) have been chosen to be investigated in this study. The hygroscopic properties of sodium halide sub-micrometre particles covered with organic acids have been examined by Fourier-transform infrared spectroscopy in an aerosol flow cell. Covered particles were generated by flowing atomized sodium halide particles (either dry or aqueous) through a heated oven containing the gaseous acid. The obtained results indicate that gaseous organic acids easily nucleate onto dry and aqueous sodium halide particles. On the other hand, scanning electron microscopy (SEM) images indicate that lauric acid coating on NaCl particles makes them to aggregate in small clusters. The hygroscopic behaviour of covered sodium halide particles in deliquescence mode shows different features with the exchange of the halide ion, whereas the organic surfactant has little effect in NaBr particles, NaCl and NaI covered particles experience appreciable shifts in their deliquescence relative humidities, with different trends observed for each of the acids studied. In efflorescence mode, the overall effect of the organic covering is to retard the loss of water in the particles. It has been observed that the presence of gaseous water in heterogeneously nucleated particles tends to displace the cover of hexanoic acid to energetically stabilize the system.

Energetics and Structural Characterization of the large-scale Functional Motion of Adenylate Kinase

Adenylate Kinase (AK) is a signal transducing protein that regulates cellular energy homeostasis balancing between different conformations. An alteration of its activity can lead to severe pathologies such as heart failure, cancer and neurodegenerative diseases. A comprehensive elucidation of the large-scale conformational motions that rule the functional mechanism of this enzyme is of great value to guide rationally the development of new medications. Here using a metadynamics-based computational protocol we elucidate the thermodynamics and structural properties underlying the AK functional transitions. The free energy estimation of the conformational motions of the enzyme allows characterizing the sequence of events that regulate its action. We reveal the atomistic details of the most relevant enzyme states, identifying residues such as Arg119 and Lys13, which play a key role during the conformational transitions and represent druggable spots to design enzyme inhibitors. Our study offers tools that open new areas of investigation on large-scale motion in proteins.