Whole Building Efficiency for Whole Foods: Preprint

The National Renewable Energy Laboratory partnered with Whole Foods Market under the Commercial Building Partnership (CBP) program to design and implement a new store in Raleigh, North Carolina. The result was a design with a predicted energy savings of 40% over ASHRAE Standard 90.1-2004, and 25% energy savings over their standard design. Measured performance of the as-built building showed that the building did not achieve the predicted performance. A detailed review of the project several months after opening revealed a series of several items in construction and controls items that were not implemented properly and were not fully corrected in the commissioning process

Thinking Like a Whole Building: A Whole Foods Market New Construction Case Study

Whole Foods Market participates in the U.S. Department of Energy's Commercial Building Partnerships (CBP) to identify and develop cost-effective, readily deployed, replicable energy efficiency measures (EEMs) for commercial buildings. Whole Foods Market is working with the National Renewable Energy Laboratory (NREL) on a retrofit and a new construction CBP project. Whole Foods Market's CBP new construction project is a standalone store in Raleigh, North Carolina. Whole Foods Market examined the energy systems and the interactions between those systems in the design for the new Raleigh store. Based on this collaboration and preliminary energy modeling, Whole Foods Market and NREL identified a number of cost-effective EEMs that can be readily deployed in other Whole Foods Market stores and in other U.S. supermarkets. If the actual savings in the Raleigh store - which NREL will monitor and verify - match the modeling results, each year this store will save nearly $100,000 in operating costs (Raleigh's rates are about$0.06/kWh for electricity and $0.83/therm for natural gas). The store will also use 41% less energy than a Standard 90.1-compliant store and avoid about 3.7 million pounds of carbon dioxide emissions

Effects of Solubilization on the Structure and Function of the Sensory Rhodopsin II/Transducer Complex

Lipid-protein interactions are known to play a crucial role in structure and physiological activity of integral membrane proteins. However, current technology for membrane protein purification necessitates extraction from the membrane into detergent micelles. Also, due to experimental protocols, most of the data available for membrane proteins is obtained using detergent-solubilized samples. Stable solubilization of membrane proteins is therefore an important issue in biotechnology as well as in biochemistry and structural biology. An understanding of solubilization effects on structural and functional properties of specific proteins is of utmost relevance for the evaluation and interpretation of experimental results. In this study, a comparison of structural and kinetic data obtained for the archaebacterial photoreceptor/transducer complex from Natronomonas pharaonis (NpSRII/NpHtrII) in detergent-solubilized and lipid-reconstituted states is presented. Laser flash photolysis, fluorescence spectroscopy, and electron paramagnetic resonance spectroscopy data reveal considerable influence of solubilization on the photocycle kinetics of the receptor protein and on the structure of the transducer protein. Especially the protein-membrane proximal region and the protein-protein interfacial domains are sensitive towards non-native conditions. These data demonstrate that relevance of biochemical and structural information obtained from solubilized membrane proteins or membrane protein complexes has to be evaluated carefully

Effects of Solubilization on the Structure and Function of the Sensory Rhodopsin II/Transducer Complex

Lipid-protein interactions are known to play a crucial role in structure and physiological activity of integral membrane proteins. However, current technology for membrane protein purification necessitates extraction from the membrane into detergent micelles. Also, due to experimental protocols, most of the data available for membrane proteins is obtained using detergent-solubilized samples. Stable solubilization of membrane proteins is therefore an important issue in biotechnology as well as in biochemistry and structural biology. An understanding of solubilization effects on structural and functional properties of specific proteins is of utmost relevance for the evaluation and interpretation of experimental results. In this study, a comparison of structural and kinetic data obtained for the archaebacterial photoreceptor/transducer complex from Natronomonas pharaonis (NpSRII/NpHtrII) in detergent-solubilized and lipid-reconstituted states is presented. Laser flash photolysis, fluorescence spectroscopy, and electron paramagnetic resonance spectroscopy data reveal considerable influence of solubilization on the photocycle kinetics of the receptor protein and on the structure of the transducer protein. Especially the protein-membrane proximal region and the protein-protein interfacial domains are sensitive towards non-native conditions. These data demonstrate that relevance of biochemical and structural information obtained from solubilized membrane proteins or membrane protein complexes has to be evaluated carefully