ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Geophysics
  • Models, Molecular
  • 2010-2014
  • 1995-1999  (41)
  • 1995  (41)
  • 1
    facet.materialart.
    Unknown
    Stratospheric Ozone Intercomparison Campaign (STOIC) 1989: Overview (1995)
    In:  CASI
    Details
    Publication Date: 2019-07-13
    Description: The NASA Upper Atmosphere Research Program organized a Stratospheric Ozone Intercomparison Campaign (STOIC) held in July-August 1989 at the Table Mountain Facility (TMF) of the Jet Propulsion Laboratory (JPL). The primary instruments participating in this campaign were several that had been developed by NASA for the Network for the Detection of Stratospheric Change: the JPL ozone lidar at TMF, the Goddard Space Flight Center trailer-mounted ozone lidar which was moved to TMF for this comparison, and the Millitech/LaRC microwave radiometer. To assess the performance of these new instruments, a validation/intercomparison campaign was undertaken using established techniques: balloon ozonesondes launched by personnel from the Wallops Flight Facility and from NOAA Geophysical Monitoring for Climate Change (GMCC) (now Climate Monitoring and Diagnostics Laboratory), a NOAA GMCC Dobson spectrophotometer, and a Brewer spectrometer from the Atmospheric Environment Service of Canada, both being used for column as well as Umkehr profile retrievals. All of these instruments were located at TMF and measurements were made as close together in time as possible to minimize atmospheric variability as a factor in the comparisons. Daytime rocket measurements of ozone were made by Wallops Flight Facility personnel using ROCOZ-A instruments launched from San Nicholas Island. The entire campaign was conducted as a blind intercomparison, with the investigators not seeing each others data until all data had been submitted to a referee and archived at the end of the 2-week period (July 20 to August 2, 1989). Satellite data were also obtained from the Stratospheric Aerosol and Gas Experiment (SAGE 2) aboard the Earth Radiation Budget Satellite and the Total Ozone Mapping Spectrometer (TOMS) aboard Nimbus 7. An examination of the data has found excellent agreement among the techniques, especially in the 20- to 40-km range. As expected, there was little atmospheric variability during the intercomparison, allowing for detailed statistical comparisons at a high level of precision. This overview paper summarizes the campaign and provides a 'road map' to subsequent papers in this issue by the individual instrument teams which will present more detailed analysis of the data and conclusions.
    Keywords: Geophysics
    Type: NASA-CR-203123 , NAS 1.26:203123 , Paper-95JD00509 , Journal of Geophysical Research (ISSN 0148-0227); 100; D5; 9193-9207
    Format: application/pdf
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    NASA TECHNICAL REPORTS
  • 2
    facet.materialart.
    Unknown
    Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: The Tat protein of bovine immunodeficiency virus (BIV) binds to its target RNA, TAR, and activates transcription. A 14-amino acid arginine-rich peptide corresponding to the RNA-binding domain of BIV Tat binds specifically to BIV TAR, and biochemical and in vivo experiments have identified the amino acids and nucleotides required for binding. The solution structure of the RNA-peptide complex has now been determined by nuclear magnetic resonance spectroscopy. TAR forms a virtually continuous A-form helix with two unstacked bulged nucleotides. The peptide adopts a beta-turn conformation and sits in the major groove of the RNA. Specific contacts are apparent between critical amino acids in the peptide and bases and phosphates in the RNA. The structure is consistent with all biochemical data and demonstrates ways in which proteins can recognize the major groove of RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Puglisi, J D -- Chen, L -- Blanchard, S -- Frankel, A D -- AI08591/AI/NIAID NIH HHS/ -- AI29135/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1200-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, Santa Cruz 95064, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502045" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Composition ; Base Sequence ; Gene Products, tat/*chemistry/metabolism ; Hydrogen Bonding ; Immunodeficiency Virus, Bovine/*chemistry ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Conformation ; Protein Structure, Secondary ; RNA, Viral/*chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 3
    facet.materialart.
    Unknown
    Galilean Satellite Observation Plans for the Near Infrared (1995)
    In:  Other Sources
    Details
    Publication Date: 2018-06-08
    Description: The Galileo spacecraft's Near-Infrared Mapping Spectrometer.
    Keywords: Geophysics
    Type: Journal of Geophysical Research
    Format: text
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    NASA TECHNICAL REPORTS
  • 4
    facet.materialart.
    Unknown
    Subdaily Northern Hemisphere Ionospheric Maps Using an Extensive Network of GPS Receivers (1995)
    In:  Other Sources
    Details
    Publication Date: 2018-06-08
    Description: Ionospheric total electron content (TEC) data derived from dual- frequency Global Positioning System (GPS) signals from 30 globally distributed network sites are fit to a simple ionospheric shell model, yielding a map of the ionosphere in the northern hemisphere every 12 hours during the January 1-15, 1993, period.
    Keywords: Geophysics
    Type: Radio Science
    Format: text
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    NASA TECHNICAL REPORTS
  • 5
    facet.materialart.
    Unknown
    On the Azimuthal Variation of Core Plasma in the Equatorial Magnetosphere (1995)
    In:  CASI
    Details
    Publication Date: 2019-08-15
    Description: Previous results of plasmapause position surveys have been synthesized into a description of the underlying global distribution of plasmasphere-like or core plasma densities unique to a steady state magnetosphere. Under these steady conditions, the boundary between high- and low-density regions is taken to represent the boundary between diurnal near-corotation and large-scale circulation streamlines that traverse the entire magnetosphere. Results indicate a boundary that has a pronounced bulge in the dusk sector that is rotated westward and markedly reduced in size at increased levels of geomagnetic activity (and presumably magnetospheric convection). The derived profile is empirical confirmation of an underlying 'tear drop' distribution of core plasma, which is valid only for prolonged steady conditions and is somewhat different from that associated with the simple superposition of sunward flow and corotation, both in its detailed shape and in its varying orientation. Variation away from the tear drop profile suggests that magnetospheric circulation departs from a uniform flow field, having a radial dependence with respect to the Earth that is qualitatively consistent with electrostatic shielding of the convection electric field and which is rotated westward at increased levels of geophysical activity.
    Keywords: Geophysics
    Type: NASA-CR-204858 , NAs 1.26:204858 , Paper-95JA02100 , Journal of Geophysical Research (ISSN 0148-0227); 100; A12; 23,597-23,605
    Format: application/pdf
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    NASA TECHNICAL REPORTS
  • 6
    facet.materialart.
    Unknown
    Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-28
    Description: DCoH, the dimerization cofactor of hepatocyte nuclear factor-1, stimulates gene expression by associating with specific DNA binding proteins and also catalyzes the dehydration of the biopterin cofactor of phenylalanine hydroxylase. The x-ray crystal structure determined at 3 angstrom resolution reveals that DCoH forms a tetramer containing two saddle-shaped grooves that comprise likely macromolecule binding sites. Two equivalent enzyme active sites flank each saddle, suggesting that there is a spatial connection between the catalytic and binding activities. Structural similarities between the DCoH fold and nucleic acid-binding proteins argue that the saddle motif has evolved to bind diverse ligands or that DCoH unexpectedly may bind nucleic acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Endrizzi, J A -- Cronk, J D -- Wang, W -- Crabtree, G R -- Alber, T -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):556-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720-3206, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725101" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Computer Graphics ; Crystallography, X-Ray ; Gene Expression Regulation ; Hydro-Lyases/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Rats ; Recombinant Fusion Proteins/chemistry/metabolism ; Transcription Factors/*chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 7
    facet.materialart.
    Unknown
    Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-10
    Description: The crystal structure of the tungsten-containing aldehyde ferredoxin oxidoreductase (AOR) from Pyrococcus furiosus, a hyperthermophilic archaeon (formerly archaebacterium) that grows optimally at 100 degrees C, has been determined at 2.3 angstrom resolution by means of multiple isomorphous replacement and multiple crystal form averaging. AOR consists of two identical subunits, each containing an Fe4S4 cluster and a molybdopterin-based tungsten cofactor that is analogous to the molybdenum cofactor found in a large class of oxotransferases. Whereas the general features of the tungsten coordination in this cofactor were consistent with a previously proposed structure, each AOR subunit unexpectedly contained two molybdopterin molecules that coordinate a tungsten by a total of four sulfur ligands, and the pterin system was modified by an intramolecular cyclization that generated a three-ringed structure. In comparison to other proteins, the hyperthermophilic enzyme AOR has a relatively small solvent-exposed surface area, and a relatively large number of both ion pairs and buried atoms. These properties may contribute to the extreme thermostability of this enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, M K -- Mukund, S -- Kletzin, A -- Adams, M W -- Rees, D C -- 1F32 GM15006/GM/NIGMS NIH HHS/ -- GM50775/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Mar 10;267(5203):1463-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, Pasadena, CA 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7878465" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehyde Oxidoreductases/*chemistry/metabolism ; Amino Acid Sequence ; Archaea/*enzymology ; Binding Sites ; *Coenzymes ; Computer Graphics ; Crystallography, X-Ray ; Enzyme Stability ; Ferrous Compounds ; Metalloproteins/analysis/chemistry ; Models, Molecular ; Molecular Sequence Data ; Organometallic Compounds/analysis/*chemistry ; Oxidation-Reduction ; Protein Conformation ; Protein Structure, Secondary ; Pteridines/analysis/chemistry ; Pterins/analysis/*chemistry ; Surface Properties ; Temperature ; Tungsten/analysis/*chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 8
    facet.materialart.
    Unknown
    Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-10
    Description: The p53 protein is a tetrameric transcription factor that plays a central role in the prevention of neoplastic transformation. Oligomerization appears to be essential for the tumor suppressing activity of p53 because oligomerization-deficient p53 mutants cannot suppress the growth of carcinoma cell lines. The crystal structure of the tetramerization domain of p53 (residues 325 to 356) was determined at 1.7 angstrom resolution and refined to a crystallographic R factor of 19.2 percent. The monomer, which consists of a beta strand and an alpha helix, associates with a second monomer across an antiparallel beta sheet and an antiparallel helix-helix interface to form a dimer. Two of these dimers associate across a second and distinct parallel helix-helix interface to form the tetramer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jeffrey, P D -- Gorina, S -- Pavletich, N P -- CA08748-29/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Mar 10;267(5203):1498-502.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7878469" target="_blank"〉PubMed〈/a〉
    Keywords: Computer Graphics ; Crystallography, X-Ray ; DNA/metabolism ; Hydrogen Bonding ; Macromolecular Substances ; Models, Molecular ; *Protein Conformation ; Protein Structure, Secondary ; Tumor Suppressor Protein p53/*chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 9
    facet.materialart.
    Unknown
    Architectures of class-defining and specific domains of glutamyl-tRNA synthetase (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-31
    Description: The crystal structure of a class I aminoacyl-transfer RNA synthetase, glutamyl-tRNA synthetase (GluRS) from Thermus thermophilus, was solved and refined at 2.5 A resolution. The amino-terminal half of GluRS shows a geometrical similarity with that of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) of the same subclass in class I, comprising the class I-specific Rossmann fold domain and the intervening subclass-specific alpha/beta domain. These domains were found to have two GluRS-specific, secondary-structure insertions, which then participated in the specific recognition of the D and acceptor stems of tRNA(Glu) as indicated by mutagenesis analyses based on the docking properties of GluRS and tRNA. In striking contrast to the beta-barrel structure of the GlnRS carboxyl-terminal half, the GluRS carboxyl-terminal half displayed an all-alpha-helix architecture, an alpha-helix cage, and mutagenesis analyses indicated that it had a role in the anticodon recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nureki, O -- Vassylyev, D G -- Katayanagi, K -- Shimizu, T -- Sekine, S -- Kigawa, T -- Miyazawa, T -- Yokoyama, S -- Morikawa, K -- New York, N.Y. -- Science. 1995 Mar 31;267(5206):1958-65.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biochemistry, School of Science, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701318" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acyl-tRNA Synthetases/chemistry ; Anticodon ; Biological Evolution ; Computer Graphics ; Crystallography, X-Ray ; Escherichia coli/enzymology ; Glutamate-tRNA Ligase/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA, Transfer, Glu/chemistry/metabolism ; Sequence Alignment ; Thermus thermophilus/*enzymology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 10
    facet.materialart.
    Unknown
    Navigating the folding routes (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolynes, P G -- Onuchic, J N -- Thirumalai, D -- New York, N.Y. -- Science. 1995 Mar 17;267(5204):1619-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Chemical Sciences, University of Illinois, Urbana 61801.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7886447" target="_blank"〉PubMed〈/a〉
    Keywords: Computer Simulation ; Models, Chemical ; Models, Molecular ; Protein Conformation ; *Protein Folding ; Protein Structure, Secondary ; Temperature ; Thermodynamics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...