Electric power supply and demand 1979 to 1988 for the contiguous United States as projected by the Regional Electric Reliability Councils in their April 1, 1979 long-range coordinated planning reports to the Department of Energy

Information concerning bulk electric power supply and demand is summarized and reviewed. Electric-utility power-supply systems are composed of power sources, transmission and distribution facilities, and users of electricity. In the United States there are three such systems of large geographic extent that together cover the entire country. Subjects covered are: energy forecasts, peak demand forecasts, generating-capacity forecasts, purchases and sales of capacity, and transmission. Extensive data are compiled in 17 tables. Information in two appendices includes a general description of the Regional Electric Reliability Councils and US generating capacity as of June 30, 1979. 3 figures, 17 tables

Investigating Therapeutic Protein Structure with Diethylpyrocarbonate Labeling and Mass Spectrometry

Protein therapeutics are rapidly transforming the pharmaceutical industry. Unlike for small molecule therapeutics, current technologies are challenged to provide the rapid, high-resolution analyses of protein higher order structures needed to ensure drug efficacy and safety. Consequently, significant attention has turned to developing new methods that can quickly, accurately, and reproducibly characterize the three-dimensional structure of protein therapeutics. In this work, we describe a method that uses diethylpyrocarbonate (DEPC) labeling and mass spectrometry to detect three-dimensional structural changes in therapeutic proteins that have been exposed to degrading conditions. Using β2-microglobulin, immunoglobulin G1, and human growth hormone as model systems, we demonstrate that DEPC labeling can identify both specific protein regions that mediate aggregation and those regions that undergo more subtle structural changes upon mishandling of these proteins. Importantly, DEPC labeling is able to provide information for up to 30% of the surface residues in a given protein, thereby providing excellent structural resolution. Given the simplicity of the DEPC labeling chemistry and the relatively straightforward mass spectral analysis of DEPC-labeled proteins, we expect this method should be amenable to a wide range of protein therapeutics and their different formulations