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  • Polymer and Materials Science  (4)
  • Molecular Sequence Data  (2)
  • 2000-2004  (2)
  • 1980-1984  (4)
  • 1
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    Isolating "uncultivable" microorganisms in pure culture in a simulated natural environment (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-11
    Description: The majority (〉99%) of microorganisms from the environment resist cultivation in the laboratory. Ribosomal RNA analysis suggests that uncultivated organisms are found in nearly every prokaryotic group, and several divisions have no known cultivable representatives. We designed a diffusion chamber that allowed the growth of previously uncultivated microorganisms in a simulated natural environment. Colonies of representative marine organisms were isolated in pure culture. These isolates did not grow on artificial media alone but formed colonies in the presence of other microorganisms. This observation may help explain the nature of microbial uncultivability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaeberlein, T -- Lewis, K -- Epstein, S S -- New York, N.Y. -- Science. 2002 May 10;296(5570):1127-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biology Department, Northeastern University, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004133" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/classification/cytology/*growth & development/*isolation & purification ; *Bacteriological Techniques ; Colony Count, Microbial ; Culture Media ; DNA, Bacterial/analysis/genetics ; DNA, Ribosomal/analysis/genetics ; Diffusion Chambers, Culture ; Geologic Sediments/*microbiology ; Molecular Sequence Data ; RNA, Ribosomal, 16S/genetics ; *Seawater ; Silicon Dioxide
    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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    Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-26
    Description: The organization of myosin into motile cellular structures requires precise temporal and spatial regulation. Proteins containing a UCS (UNC-45/CRO1/She4p) domain are necessary for the incorporation of myosin into the contractile ring during cytokinesis and into thick filaments during muscle development. We report that the carboxyl-terminal regions of UNC-45 bound and exerted chaperone activity on the myosin head. The amino-terminal tetratricopeptide repeat domain of UNC-45 bound the molecular chaperone Hsp90. Thus, UNC-45 functions both as a molecular chaperone and as an Hsp90 co-chaperone for myosin, which can explain previous findings of altered assembly and decreased accumulation of myosin in UNC-45 mutants of Caenorhabditis elegans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barral, Jose M -- Hutagalung, Alex H -- Brinker, Achim -- Hartl, F Ulrich -- Epstein, Henry F -- New York, N.Y. -- Science. 2002 Jan 25;295(5555):669-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11809970" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Binding Sites ; Caenorhabditis elegans/genetics/*metabolism ; Caenorhabditis elegans Proteins/chemistry/genetics/*metabolism ; Cell Line ; Cloning, Molecular ; HSP70 Heat-Shock Proteins/genetics/metabolism ; HSP90 Heat-Shock Proteins/genetics/metabolism ; Molecular Chaperones/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Myosins/*metabolism ; Peptide Fragments/metabolism ; Protein Binding ; Protein Structure, Tertiary ; Recombinant Proteins/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)
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  • 3
    Electronic Resource
    Electronic Resource
    Kinetics of nucleic acid-large ligand interactions: Multiplet-closure approximations and matrix-iteration techniques (1981)
    New York : Wiley-Blackwell
    Biopolymers 20 (1981), S. 1651-1669 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Approximate methods are developed and evaluated for treating the rate of binding ligands that cover several contiguous sites to a homogeneous one-dimensional lattice, which represents a nucleic acid or other linear biopolymer. The model requires as input only the number of lattice sites necessary for binding, the total number (possibly infinite) of lattice sites, and elementary rate constants for the cooperative and noncooperative association and dissociation of the ligand on the lattice. The computational methods employed are an extension of the triplet closure approximation from the helix-coil (single-site ligand) problem to the large ligand binding problem. It is found that consideration of clusters of n + 2 lattice sites, where each ligand covers n sites, gives a surprisingly accurate description of the kinetics. The approximation is implemented by an extension of the matrix-iteration approach proposed by Craig and Crothers. The effects of the finite lattice length, as well as the capability to treat ligand motion along the lattice, are incorporated. When all symmetries are taken into consideration, the time required for the matrix iteration calculation rises only linearly with the ligand length n and is considerably less than that of the Monte Carlo method, which is used as a standard for comparison.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1981.360200808
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  • 4
    Electronic Resource
    Electronic Resource
    Kinetics of irreversible dissociation for proteins bound cooperatively to DNA (1984)
    New York : Wiley-Blackwell
    Biopolymers 23 (1984), S. 1249-1259 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: We consider the irreversible dissociation kinetics of proteins that bind cooperatively and nonspecifically to DNA. Our model consists of an infinitely long one-dimensional nucleic acid lattice on which are bound protein ligands. A set of adjacent bound proteins forms a cluster of length n. A protein molecule may dissociate from any site within the bound cluster, not only from the ends, as was assumed in a previous model of this process due to Lohman [(1983) Biopolymers 22, 1697-1713]. By considering this additional pathway, we present a more general treatment of the dissociation kinetics of cooperatively bound ligands. We show that dissociation from the (n-2) internal positions of an n-cluster is an important pathway when the initial fractional saturation of the lattice is close to unity and the co operatively is low. When the fractional saturation is initially equal to 1 and the co operatively is low, our model does not give the zero-order dissociation kinetics predicted by the Lohman model.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360230709
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  • 5
    Electronic Resource
    Electronic Resource
    Environmental stress crack growth in medium-density polyethylene pipe (1981)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 26 (1981), S. 1049-1056 
    Details
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/app.1981.070260327
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  • 6
    Electronic Resource
    Electronic Resource
    Continuous extrusion of high-modulus semicrystalline polymers (1981)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 26 (1981), S. 395-409 
    Details
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: A process has been developed by which very high-modulus semicrystalline polymer films can be extruded continuously from a melt. This is accomplished by controlled cooling of the melt in a two-stage flow channel. A temperature gradient along the flow channel quenches the melt prior to an area reduction in which the polymer undergoes solid-state orientation. Analysis of high-density polyethylene tapes extruded by this process shows that they have properties similar to samples hydrostatically extruded at 120°C. Infrared analysis was used to determine both the degree of crystallinity and degree of orientation in these tapes as well as previously prepared hydrostatically extruded samples.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/app.1981.070260202
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