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Burial of gas-phase HNO(3) by growing ice surfaces under tropospheric conditions.

The uptake of gas-phase nitric acid by ice surfaces undergoing growth by vapor deposition has been performed for the first time under conditions of the free troposphere. The investigation was performed using a coated-wall flow tube coupled to a chemical ionization mass spectrometer, at nitric acid partial pressures between 10(-7) and 10(-6) hPa, at 214, 229 and 239 K. Ice surfaces were prepared as smooth ice films from ultra-pure water. During the experiments an excess flow of water vapor was added to the carrier gas flow and the existing ice surfaces grew by depositing water vapor. The average growth rates ranged from 0.7-5 microm min(-1), values similar to those which prevail in some portions of the atmosphere. With growing ice the long term uptake of nitric acid is significantly enhanced compared to an experiment performed at equilibrium, i.e. at 100% relative humidity (RH) with respect to ice. The fraction of HNO(3) that is deposited onto the growing ice surface is independent of the growth rate and may be driven by the solubility of the nitric acid in the growing ice film rather than by condensation kinetics alone.

Atmosphere↗

Mutagenesis-based definitions and probes of residue burial in proteins.

Every residue of the 101-aa Escherichia coli toxin CcdB was substituted with Ala, Asp, Glu, Lys, and Arg by using site-directed mutagenesis. The activity of each mutant in vivo was characterized as a function of Controller of Cell Division or Death B protein (CcdB) transcriptional level. The mutation data suggest that an accessibility value of 5% is an appropriate cutoff for definition of buried residues. At all buried positions, introduction of Asp results in an inactive phenotype at all CcdB transcriptional levels. The average amount of destabilization upon substitution at buried positions decreases in the order Asp>Glu>Lys>Arg>Ala. Asp substitutions at buried sites in two other proteins, maltose-binding protein and thioredoxin, also were shown to be severely destabilizing. Ala and Asp scanning mutagenesis, in combination with dose-dependent expression phenotypes, was shown to yield important information on protein structure and activity. These results also suggest that such scanning mutagenesis data can be used to rank order sequence alignments and their corresponding homology models, as well as to distinguish between correct and incorrect structural alignments. With continuous reductions in oligonucleotide costs and increasingly efficient site-directed mutagenesis procedures, comprehensive scanning mutagenesis experiments for small proteins/domains are quite feasible.

Bacterial Proteins↗