International audienceThis paper reviews recent progress in the development of the Beijing Climate Center Climate System Model (BCC_CSM) and its four component models (atmosphere, land surface, ocean, and sea ice). Two recent versions are described: BCC_CSM1.1 with coarse resolution (approximately 2.8125°×2.8125°) and BCC_CSM1.1(m) with moderate resolution (approximately 1.125°×1.125°). Both versions are fully coupled climate-carbon cycle models that simulate the global terrestrial and oceanic carbon cycles and include dynamic vegetation. Both models well simulate the concentration and temporal evolution of atmospheric CO2 during the 20th century with anthropogenic CO2 emissions prescribed. Simulations using these two versions of the BCC_CSM model have been contributed to the Coupled Model Intercomparison Project phase five (CMIP5) in support of the Intergovernmental Panel on Climate Change (IPCC) Fifth Assessment Report (AR5). These simulations are available for use by both national and international communities for investigating global climate change and for future climate projections.Simulations of the 20th century climate using BCC_CSM1.1 and BCC_CSM1.1(m) are presented and validated, with particular focus on the spatial pattern and seasonal evolution of precipitation and surface air temperature on global and continental scales. Simulations of climate during the last millennium and projections of climate change during the next century are also presented and discussed. Both BCC_CSM1.1 and BCC_CSM1.1(m) perform well when compared with other CMIP5 models. Preliminary analyses indicate that the higher resolution in BCC_CSM1.1(m) improves the simulation of mean climate relative to BCC_CSM1.1, particularly on regional scales

Partition and transportation of drug in the plasma membrane of a mammalian cell are the prerequisite for its function on target protein. Therefore, comprehensive understanding of the physicochemical properties and mechanism behind these complex phenomena is crucial in pharmaceutical research. By using the state-of-art molecular simulations with polarization effect implicitly or explicitly included, we studied the permeation behavior of 2-aminoethoxydiphenyl borate (2-APB), a broad-spectrum modulator for a number of membrane proteins. We showed that the protonation state and therefore the polarity of the drug is critical for its partition, and that the drug is likely to switch between different protonation states along its permeation pathway. By changing the degrees of freedom, protonation further affects the thermodynamic of the permeation pathway of 2-APB, leading to different entropic contributions. A survey on 54 analog structures with similar backbone to 2-APB showed that delicate balance between entropy and polarity plays an important role in drugs’ potency.

No abstract

No abstract