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  • Cattle  (4)
  • American Association for the Advancement of Science (AAAS)  (4)
  • American Institute of Physics
  • 1995-1999  (1)
  • 1990-1994  (3)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (4)
  • American Institute of Physics
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Year
  • 1
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    Attomole protein characterization by capillary electrophoresis-mass spectrometry (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-30
    Description: Electrospray ionization with an ultralow flow rate (〈/=4 nanoliters per minute) was used to directly couple capillary electrophoresis with tandem mass spectrometry for the analysis and identification of biomolecules in mixtures. A Fourier transform mass spectrometer provided full spectra (〉30 kilodaltons) at a resolving power of approximately 60,000 for injections of 0.7 x 10(-18) to 3 x 10(-18) mole of 8- to 29-kilodalton proteins with errors of 〈1 dalton in molecular mass. Using a crude isolate from human blood, a value of 28,780.6 daltons (calculated, 28,780.4 daltons) was measured for carbonic anhydrase, representing 1 percent by weight of the protein in a single red blood cell. Dissociation of molecular ions from 9 x 10(-18) mole of carbonic anhydrase gave nine sequence-specific fragment ions, more data than required for unique retrieval of this enzyme from the protein database.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Valaskovic, G A -- Kelleher, N L -- McLafferty, F W -- 08-T2GM07273/GM/NIGMS NIH HHS/ -- GM16609/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1199-202.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Baker Laboratory, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703047" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carbonic Anhydrases/*analysis/chemistry ; Cattle ; Cytochrome c Group/analysis/chemistry ; Electrophoresis, Capillary/*methods ; Horses ; Humans ; Mass Spectrometry/*methods ; Molecular Weight ; Proteins/*analysis/chemistry ; Sensitivity and Specificity ; Spectroscopy, Fourier Transform Infrared ; Ubiquitins/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)
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  • 2
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    Inclusion of thermal motion in crystallographic structures by restrained molecular dynamics (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-07
    Description: A protein crystal structure is usually described by one single structure, which largely omits the dynamical behavior of the molecule. A molecular dynamics method with a time-averaged crystallographic restraint was used to overcome this limitation. This method yields an ensemble of structures in which all possible thermal motions are allowed, that is, in additional to isotropic distributions, anisotropic and anharmonic positional distributions occur as well. In the case of bovine pancreatic phospholipase A2, this description markedly improves agreement with the observed x-ray diffraction data compared to the results of the classical one-model structure description. Time-averaged crystallographically restrained molecular dynamics reveals large mobilities in the loops involved in lipid bilayer association.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gros, P -- van Gunsteren, W F -- Hol, W G -- New York, N.Y. -- Science. 1990 Sep 7;249(4973):1149-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉BIOSON Research Institute, University of Groningen, The Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2396108" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Crystallography ; Hot Temperature ; Models, Molecular ; Motion ; *Phospholipases ; *Phospholipases A ; Phospholipases A2 ; Protein Conformation ; X-Ray Diffraction
    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)
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  • 3
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    Cloning and expression of the cDNA for human gamma-glutamyl carboxylase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-13
    Description: The cDNA for human gamma-glutamyl carboxylase, which accomplishes the post-translational modification required for the activity of all of the vitamin K-dependent proteins, was cloned. The enzyme is a 758-residue integral membrane protein and appears to have three transmembrane domains near its amino terminus. The hydrophilic COOH-terminal half of the carboxylase has 19.3 percent identity with soybean seed lipoxygenase. Expression of the cloned cDNA resulted in an increase in carboxylase activity in microsomes of transfected cells compared to mock-transfected cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, S M -- Cheung, W F -- Frazier, D -- Stafford, D W -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1634-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of North Carolina, Chapel Hill 27599-3280.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1749935" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; *Carbon-Carbon Ligases ; Cattle ; Cloning, Molecular ; DNA/genetics ; Humans ; Ligases/*genetics ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry ; Polymerase Chain Reaction ; Recombinant Proteins ; Sequence Alignment
    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)
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  • 4
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    The hydrolytic water molecule in trypsin, revealed by time-resolved Laue crystallography (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-29
    Description: Crystals of bovine trypsin were acylated at the reactive residue, serine 195, to form the transiently stable p-guanidinobenzoate. Hydrolysis of this species was triggered in the crystals by a jump in pH. The hydrolysis was monitored by three-dimensional Laue crystallography, resulting in three x-ray diffraction structures, all from the same crystal and each representing approximately 5 seconds of x-ray exposure. The structures were analyzed at a nominal resolution of 1.8 angstroms and were of sufficient quality to reproduce subtle features in the electron-density maps for each of the structures. Comparison of the structures before and after the pH jump reveals that a water molecule has positioned itself to attack the acyl group in the initial step of the hydrolysis of this transient intermediate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Singer, P T -- Smalas, A -- Carty, R P -- Mangel, W F -- Sweet, R M -- New York, N.Y. -- Science. 1993 Jan 29;259(5095):669-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biology Department, Argonne National Laboratory, IL 60439.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430314" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cattle ; Crystallography/methods ; Indicators and Reagents ; Models, Molecular ; *Protein Conformation ; Serine ; Trypsin/*chemistry ; Water
    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
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