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  • 1
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    Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-09
    Description: The three-dimensional structure of an active, disulfide cross-linked dimer of the ligand-binding domain of the Salmonella typhimurium aspartate receptor and that of an aspartate complex have been determined by x-ray crystallographic methods at 2.4 and 2.0 angstrom (A) resolution, respectively. A single subunit is a four-alpha-helix bundle with two long amino-terminal and carboxyl-terminal helices and two shorter helices that form a cylinder 20 A in diameter and more than 70 A long. The two subunits in the disulfide-bonded dimer are related by a crystallographic twofold axis in the apo structure, but by a noncrystallographic twofold axis in the aspartate complex structure. The latter structure reveals that the ligand binding site is located more than 60 A from the presumed membrane surface and is at the interface of the two subunits. Aspartate binds between two alpha helices from one subunit and one alpha helix from the other in a highly charged pocket formed by three arginines. The comparison of the apo and aspartate complex structures shows only small structural changes in the individual subunits, except for one loop region that is disordered, but the subunits appear to change orientation relative to each other. The structures of the two forms of this protein provide a step toward understanding the mechanisms of transmembrane signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milburn, M V -- Prive, G G -- Milligan, D L -- Scott, W G -- Yeh, J -- Jancarik, J -- Koshland, D E Jr -- Kim, S H -- AI 30725/AI/NIAID NIH HHS/ -- DK09765/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1342-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1660187" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aspartic Acid/metabolism ; Binding Sites ; Disulfides/analysis ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; *Receptors, Amino Acid ; Receptors, Cell Surface/*chemistry/metabolism ; Salmonella typhimurium/metabolism ; 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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  • 2
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    Three-dimensional structure of dimeric human recombinant macrophage colony-stimulating factor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-20
    Description: Macrophage colony-stimulating factor (M-CSF) triggers the development of cells of the monocyte-macrophage lineage and has a variety of stimulatory effects on mature cells of this class. The biologically active form of M-CSF is a disulfide-linked dimer that activates an intrinsic tyrosine kinase activity on the M-CSF receptor by inducing dimerization of the receptor molecules. The structure of a recombinant human M-CSF dimer, determined at 2.5 angstroms by x-ray crystallography, contains two bundles of four alpha helices laid end-to-end, with an interchain disulfide bond. Individual monomers of M-CSF show a close structural similarity to the cytokines granulocyte-macrophage colony-stimulating factor and human growth hormone. Both of these cytokines are monomeric in their active form, and their specific receptors lack intrinsic tyrosine kinase activity. The similarity of these structures suggests that the receptor binding determinants for all three cytokines may be similar.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pandit, J -- Bohm, A -- Jancarik, J -- Halenbeck, R -- Koths, K -- Kim, S H -- New York, N.Y. -- Science. 1992 Nov 20;258(5086):1358-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural Biology Division, Lawrence Berkeley Laboratory, Berkeley, CA 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1455231" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography ; Disulfides ; Granulocyte-Macrophage Colony-Stimulating Factor/ultrastructure ; Growth Hormone/chemistry ; Macrophage Colony-Stimulating Factor/*ultrastructure ; Models, Molecular ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/ultrastructure ; Sequence Homology, Amino Acid ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21 (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-02-19
    Description: The crystal structure at 2.7 A resolution of the normal human c-H-ras oncogene protein lacking a flexible carboxyl-terminal 18 residue reveals that the protein consists of a six-stranded beta sheet, four alpha helices, and nine connecting loops. Four loops are involved in interactions with bound guanosine diphosphate: one with the phosphates, another with the ribose, and two with the guanine base. Most of the transforming proteins (in vivo and in vitro) have single amino acid substitutions at one of a few key positions in three of these four loops plus one additional loop. The biological functions of the remaining five loops and other exposed regions are at present unknown. However, one loop corresponds to the binding site for a neutralizing monoclonal antibody and another to a putative "effector region"; mutations in the latter region do not alter guanine nucleotide binding or guanosine triphosphatase activity but they do reduce the transforming activity of activated proteins. The data provide a structural basis for understanding the known biochemical properties of normal as well as activated ras oncogene proteins and indicate additional regions in the molecule that may possibly participate in other cellular functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Vos, A M -- Tong, L -- Milburn, M V -- Matias, P M -- Jancarik, J -- Noguchi, S -- Nishimura, S -- Miura, K -- Ohtsuka, E -- Kim, S H -- CA 45593/CA/NCI NIH HHS/ -- GM 29287/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 19;239(4842):888-93.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkely 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2448879" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal/immunology ; Binding Sites ; Catalysis ; Crystallization ; Epitopes/immunology ; Escherichia coli/genetics ; GTP Phosphohydrolases ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Neoplasms/genetics ; Phosphates/metabolism ; Protein Conformation ; Proto-Oncogene Proteins/genetics/immunology/*metabolism ; Proto-Oncogene Proteins p21(ras) ; Recombinant Proteins/metabolism ; 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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  • 4
    Electronic Resource
    Electronic Resource
    High-resolution crystals and preliminary X-ray diffraction studies of a catalytic RNA (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 290-292 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: High-resolution single crystals of a catalytic RNA molecule derived from the sequence of the satellite RNA of tobacco ringspot virus have been obtained. The unit-cell volumes of the RNA crystals vary depending on the crystallization conditions and temperature. The best crystal form, when flash frozen, has space group P1 with unit-cell dimensions a = 53.08, b = 71.81, c = 28.03 Å, α = 98.43, β = 104.32 and γ = 74.54°. This form diffracts to a resolution of 2.4 Å. A heavy-atom derivative search is in progress.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444993013071
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  • 5
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary crystallographic analysis of the Ras binding domain of RalGDS, a guanine nucleotide dissociation stimulator of the Ral protein (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 1033-1035 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The RalGDS is a guanine nucleotide dissociation stimulator which activates the Ral protein, a Ras-like small GTPase. The C-terminal domain of the RalGDS (C-RalGDS) binds tightly to the effector loop of Ras suggesting that the RalGDS may be a crossing point of two signal tranduction pathways associated with the Ras and Ral proteins. C-RalGDS has been purified and crystallized in space group C2, with unit-cell dimensions a = 108.8, b = 30.7, c = 51.3 Å, β = 91.7° at 277 K and a = 103.8, b = 30.55, c = 51.4 Å, β = 94.9° for data collected at 100 K. The crystals diffract to 1.8 Å at a synchrotron radiation source. To use the multiple-wavelength anomalous diffraction method for phasing, a selenomethionine derivative of the protein has also been crystallized.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996003228
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  • 6
    Electronic Resource
    Electronic Resource
    Use of low-molecular-weight polyethylene glycol in the crystallization of RNA oligomers (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 764-767 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: We have crystallized a variety of RNA oligonucleotides in a form suitable for X-ray diffraction studies using polyethylene glycol with a low-molecular-weight distribution (PEG 400) as the precipitant. Crystallization experiments on a set of 26 RNA oligomers ranging from eight to 12 nucleotides in length resulted in eight diffraction-quality crystals. Of these eight RNA crystals, six utilized PEG 400 as the precipitating agent. We have also been able to obtain large single crystals of a DNA–RNA hybrid, transfer RNA (two different conditions) and a catalytic RNA from PEG 400 solutions. These results suggest that PEG 400 may be a generally useful alternative to 2-methyl-2,4-pentanediol (MPD) which has, thus far, been the most successful precipitant for DNA oligomers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994003458
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  • 7
    Electronic Resource
    Electronic Resource
    Electron heating by beam-plasma interaction in uniform magnetic field
    Amsterdam : Elsevier
    Physics Letters A 28 (1968), S. 331-332 
    Details
    ISSN: 0375-9601
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0375-9601(68)90316-2
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  • 8
    Electronic Resource
    Electronic Resource
    Sparse matrix sampling: a screening method for crystallization of proteins (1991)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 24 (1991), S. 409-411 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: A set of screening conditions for initial experiments in protein crystallization has been developed, tested, and is herein presented. These solution and precipitant conditions are empirically derived based on known or published crystallization conditions of various proteins in the past, so as to sample as large a range of buffer, pH, additive and precipitant variables as possible, using small amounts of proteins. The 50 crystallization conditions have been tested on 15 previously crystallized proteins, all of which were also crystallized in at least one form by this screen. This method is also shown to be highly successful in the crystallization of proteins which had not previously been crystallized.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889891004430
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  • 9
    Electronic Resource
    Electronic Resource
    Generation of beams of charged particles with transverse energy (1969)
    Springer
    Czechoslovak journal of physics 19 (1969), S. 964-973 
    Details
    ISSN: 1572-9486
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The paper describes the operation and construction of an electron gun designed to form beams with variable transverse energy and a variable spread of magnetic moments. Transverse energy is acquired by the electrons as the beam passes through a weakly non-adiabatic magnetic step, and in an adiabatic motion through a growing magnetic field. The small spread of magnetic moments of the beam electrons is achieved by fulfilling the so-called focusing conditions which ensure that the spread of moments resulting from different initial radii of the particles is compensated by their initial radial velocities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01690168
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  • 10
    Electronic Resource
    Electronic Resource
    Transit of beams of charged particles through a non-adiabatic magnetic field (1969)
    Springer
    Czechoslovak journal of physics 19 (1969), S. 204-216 
    Details
    ISSN: 1572-9486
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The possibility of obtaining beams of particles with high transverse energies in a strong magnetic field is discussed. The motion of particles in a weakly non-adiabatic field is described by a linear non-homogeneous equation. The non-adiabaticity of motion is caused, in the first approximation, by the curvature of the magnetic lines of force. The conditions for a small spread of magnetic moments of the beam particles are established by solving the equation of motion. The transverse energy of particles and its spread can be varied by varying the shape of the magnetic field and the initial radial velocities of the particles. As a result of the conditions for a small spread of magnetic moments, a beam traversing a steep magnetic field gains a smaller magnetic moment than a beam passing through a field with a lesser slope.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01689850
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