Paper Session II-A - Space Station Freedom Accommodation of the Human Exploration Initiative

In his July 20th speech commemorating the 20th anniversary of the first Apollo Moon landing, President Bush proposed ...a sustained program of manned exploration of the solar system...and the permanent settlement of space. The President\u27s plan for the future of America\u27s manned space program calls for Space Station Freedom to be operational in the 1990\u27s followed by a return to the Moon for the new century, this time to stay , and then a manned mission to Mars. Space Station Freedom is a fundamental part of this long-range, evolutionary, human exploration initiative. It will support continuous human presence in Earth orbit for the purposes of scientific research and the development of technologies critical to the exploration missions. In addition to serving as a research and development facility in space, Freedom will be used as a spaceport or transportation node to support the assembly, servicing and checkout of space transfer vehicles which will ferry crew and cargo to the lunar surface and on to Mars. A study conducted by NASA during the Autumn of 1989 identified exploration accommodation requirements for the Space Station and formulated plans to implement mission-supporting capabilities. It was determined that the initial Space Station Freedom configuration (termed Assembly Complete) must be augmented to provide additional resources and capabilities. Increases will be required to Freedom crew, power, pressurized volume and truss structure. New capabilities will be required such as spacecraft assembly and servicing. A significant conclusion of the 90-day NASA study was that Space Station is capable of accommodating the necessary additions due to the evolutionary nature of the design

Space Station Freedom Integrated Research and Development Growth

Space Station Freedom is designed to be an Earth-orbiting, multidiscipline research and development (R&D) facility capable of evolution to accomodate a variety of potential uses. One evolution scenario is growth to an enhanced R&D facility. In support of the Space Station Freedom Program Preliminary Design Review (PDR), the NASA Langley Research Center Space Station Office is analyzing growth requirements and evaluating configurations for this R&D utilization. This paper presents a summary of FY1989 study results including time-phased growth plans, R&D growth issues and configurations, and recommendations for the program baseline design which will facilitate evolutionary R&D growth. This study consisted of three major areas of concentration: mission requirements analysis; Space Station Freedom systems growth analysis; and growth accomodations and trades. Mission requirements analysis was performed to develop a realistic mission model of post-Phase 1 R&D missions. A systems-level analysis was performed to project incremental growth requirements of Space Station Freedom needed to support these R&D missions. Identification of growth requirements and specific growth elements led to the need for special accomodations analyses and trades. These studies included identification of hooks and scars on the baseline design, determination of an optimal module growth pattern, analysis of the dual keel length, and determination of an optimal locaton for the customer servicing facility. Results of this study show that Space Station Freedom must be capable of evolving to a dual keel, eight pressurized module configuration (two growth habs and two growth labs); providing 275 kW power (for experimenters and station housekeeping); accomodating a crew of 24; and supporting other growth structures and special facilities to meet projected R&D mission requirements

Sedimente als Lebensraum

Ahlf W, Flemming HC, Götz R, et al. Sedimente als Lebensraum. In: Calmano W, ed. Untersuchung und Bewertung von Sedimenten. Berlin: Springer; 2001: 7-65

'Iter Dalekarlicum'

Mass spectrometry based proteomics generally seeks to identify and fully characterize protein species with high accuracy and throughput. Recent improvements in protein separation have greatly expanded the capacity of top-down proteomics (TDP) to identify a large number of intact proteins. To date, TDP has been most tightly associated with Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry. Here, we couple the improved separations to a Fourier-transform instrument based not on ICR but using the Orbitrap Elite mass analyzer. Application of this platform to H1299 human lung cancer cells resulted in the unambiguous identification of 690 unique proteins and over 2000 proteoforms identified from proteins with intact masses <50 kDa. This is an early demonstration of high throughput TDP (>500 identifications) in an Orbitrap mass spectrometer and exemplifies an accessible platform for whole protein mass spectrometry

Nano-LC FTICR Tandem Mass Spectrometry for Top-Down Proteomics: Routine Baseline Unit Mass Resolution of Whole Cell Lysate Proteins up to 72 kDa

Current high-throughput top-down proteomic platforms provide routine identification of proteins less than 25 kDa with 4-D separations. This short communication reports the application of technological developments over the past few years that improve protein identification and characterization for masses greater than 25 kDa. Advances in separation science have allowed increased numbers of proteins to be identified, especially by nanoliquid chromatography (nLC) prior to mass spectrometry (MS) analysis. Further, a goal of high-throughput top-down proteomics is to extend the mass range for routine nLC MS analysis up to 80 kDa because gene sequence analysis predicts that ∼70% of the human proteome is transcribed to be less than 80 kDa. Normally, large proteins greater than 50 kDa are identified and characterized by top-down proteomics through fraction collection and direct infusion at relatively low throughput. Further, other MS-based techniques provide top-down protein characterization, however at low resolution for intact mass measurement. Here, we present analysis of standard (up to 78 kDa) and whole cell lysate proteins by Fourier transform ion cyclotron resonance mass spectrometry (nLC electrospray ionization (ESI) FTICR MS). The separation platform reduced the complexity of the protein matrix so that, at 14.5 T, proteins from whole cell lysate up to 72 kDa are baseline mass resolved on a nano-LC chromatographic time scale. Further, the results document routine identification of proteins at improved throughput based on accurate mass measurement (less than 10 ppm mass error) of precursor and fragment ions for proteins up to 50 kDa