Microclimate and ventilation in Estonian and Finnish dairy buildings

A series of ventilation, thermal and indoor air quality measurements were performed in 14 different dairy buildings in Estonia and Finland. The number of animals in the buildings varied from 30 to 600. Measurements were made all year round with ambient temperatures ranging between −40 °C and +30 °C. The results showed that microclimatic conditions in the dairy buildings were affected by the design of the building, outside temperature, wind, ventilation and manure handling method. The average inside air concentration of carbon dioxide was 950 ppm, ammonia 5 ppm, methane 48 ppm, relative humidity 70% and inside air velocity was 0.2 m/s. Although occasionally exceeded, the ventilation and average indoor air quality in the dairy buildings were mainly within the recommended limits.     

Femtosecond resonance enhanced CARS for background-free detection of organic molecules

We study the coherent excitation profile (CEP) of resonance enhanced femtosecond CARS in a model system zinc phthalocyanine in a polymer film host as a prospective technique for detection and identification of molecular species in ambient environments. A new method of suppressing the non-resonant FWM background is demonstrated. Transform theory is applied to calculate CEP based on the absorption spectrum, and good agreement between theory and experiment is obtained.     

Structural Communication between the E. coli Chaperones DnaK and Hsp90

The 70 kDa and 90 kDa heat shock proteins Hsp70 and Hsp90 are two abundant and highly conserved ATP-dependent molecular chaperones that participate in the maintenance of cellular homeostasis. In Escherichia coli, Hsp90 (Hsp90Ec) and Hsp70 (DnaK) directly interact and collaborate in protein remodeling. Previous work has produced a model of the direct interaction of both chaperones. The locations of the residues involved have been confirmed and the model has been validated. In this study, we investigate the allosteric communication between Hsp90Ec and DnaK and how the chaperones couple their conformational cycles. Using elastic network models (ENM), normal mode analysis (NMA), and a structural perturbation method (SPM) of asymmetric and symmetric DnaK-Hsp90Ec, we extract biologically relevant vibrations and identify residues involved in allosteric signaling. When one DnaK is bound, the dominant normal modes favor biological motions that orient a substrate protein bound to DnaK within the substrate/client binding site of Hsp90Ec and release the substrate from the DnaK substrate binding domain. The presence of one DnaK molecule stabilizes the entire Hsp90Ec protomer to which it is bound. Conversely, the symmetric model of DnaK binding results in steric clashes of DnaK molecules and suggests that the Hsp90Ec and DnaK chaperone cycles operate independently. Together, this data supports an asymmetric binding of DnaK to Hsp90Ec.