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  • 1990-1994  (7)
  • 1955-1959  (1)
  • 1920-1924
  • 1915-1919  (1)
  • Life and Medical Sciences  (6)
  • Polymer and Materials Science  (3)
  • 1
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 33 (1993), S. 1185-1193 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: According to the conventional definition, the hydrophobic effect is a result of thermodynamic changes occurring when a nonpolar group dissolves in water and attributable to the fact that water in contact with such a group has special structural and energetic properties. Disagreement now exists as to whether this effect promotes or hinders protein denaturation. Taking the heat capacity change of unfolding as a measure of the hydrophobicity of the protein interior, others have shown that protein stabilities are systematically affected by changes in hydrophobicity. It has been suggested that the observed trends show that hydrophobic hydration is intrinsically a destabilizing factor. Model calculations using known equations for the stability curves and certain simplifying assumptions now show that such regularities provide no evidence for or against this conclusion. All available data can be rationalized if hydrophobic terms are evaluated from models that require a positive hydrophobic contribution to the Gibbs energy of unfolding. The calculations also confirm the recent finding that any set of proteins with denaturation temperatures between about 330 and 380 K that exhibits entropy convergence at about 386 K is thermodynamically required to show enthalpy convergence at approximately the same temperature. © 1993 John Wiley & Sons, Inc.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 133 (1959), S. 219-239 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0730-2312
    Keywords: DNA/protein interaction ; simple repetitive DNA ; binding domain ; conformation changes ; intron 2 ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Electrophoretic mobility shift assays reveal that HeLa neuclear proteins bind fast and with measurable affinity to target DNAs containing mixed simple repetitive (gt)n(ga)m stretches. Preincubation of the proteins at elevated temperature prevents the formation of the major DNA/protein complex in favour of several distinct assemblies. A similar pattern of retarded bands was observed employing higher salt concentrations in binding reaction. Thus conformational changes of different proteins appear to influence the complex rather than alternating DNA structures. Separation of the total nuclear extract into a water soluble and an insoluble protein fraction leads to a complete loss of target DNA bindinlg capability of the fractions. The binding capacity is restored by combining the two fractions suggesting that at least two protein components are necessary to form a complex with the target sequence. The proteins can be differentiated into head sensitive, water soluble and temporary stable, water insoluble, respectively. Furthermore, specifically binding polypeptides are not detectable by Southwestern analyses, probably because the essential components are separated during electrophoresis. DNase 1 footpoint analyses yield four different protein binding regions only on the (gt)n(ga)m harbouring strand. The footprints cover larger portions of the mixed simple repeat in addition to a portion 5′ of the (gt)n part. Hence at lealst two nuclear protein components of unknown biological function have to be present simultaneously to protect preferentially the (gt)n(ga)m-containing strand intron 2 in HLA-DRB genes
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part B: Polymer Physics 29 (1991), S. 933-943 
    ISSN: 0887-6266
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Viscoelastic properties of styrene-co-methyl methacrylate random copolymers have been determined over a temperature range covering the glass transition, the rubbery plateau, and the terminal zone and compared with polystyrene and polymethyl methacrylate homopolymers. Nonlinear behavior was observed in the variations of most of the physical and rheological characteristics with the methyl methacrylate content in the copolymer. Results are interpreted in terms of the rupture of polar-polar intermolecular interactions between ester groups due to the presence of styrene units.
    Additional Material: 18 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Polymers for Advanced Technologies 2 (1991), S. 161-169 
    ISSN: 1042-7147
    Keywords: Crystalline interphase ; Interfacial polymer chain orientation ; Elastic modulus of interphase ; Stress-free temperature ; Reversible energy of adhesion ; 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
    Notes: The aim of this third part is to analyze the structure and properties of the interfacial region between carbon fibers and PEEK as a function of different thermal conditioning treatments. First, it is shown by means of optical microscopy that the interfacial zone is not different from the bulk matrix when standard cooling conditions are used. On the contrary, a transcrystalline interphase is formed near the carbon fiber surface in systems that have been subjected to isothermal treatments. By comparison with previous results concerning the mechanical properties of the fiber-matrix interface, it appears that the interfacial shear strength decreases in the presence of a transcrystalline interphase or when the crystallization rate of PEEK increases. Moreover, it seems that the “constraint state” of the amorphous phase of PEEK near the fiber surface could also play a role in the interfacial shear strength. Secondly, a method is proposed in order to estimate the elastic modulus of crystalline interphases. It seems that this modulus is strongly dependent on the crystallization rate of the polymer. Finally, the determination of the stress-free temperature, defined as the temperature at which a longitudinal compressive stress just appears on the carbon fiber during the processing of the composites, is performed by recording the acoustic events corresponding to the fragmentation process in single-fiber composites. The results confirm that the crystallization rate and the “constraint state” of the amorphous phase of the matrix play an important role in the mechanical behavior of carbon fiber-PEEK interfaces.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 38 (1994), S. 440-452 
    ISSN: 1040-452X
    Keywords: Spermiogenesis ; Nuclear condensation ; Chromatin ; Protamines ; Protein-precursors ; Neogastropod mollusc ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: During the process of chromatin cndensation in the spermiogenesis of the neogastropod mollusc Murex brandaris, the nuclear protein complement undergoes a complex series of changes. These changes lead to the appearance of three small protamines in the ripe sperm nuclei. We have characterized this system electrophoretically and at the compositions with antibodies elicited against a specific spermatozoan protamine. Our results indicate that the complex pattern of chromatin condensation during spermiogenesis in this species (M. brandaris) may be modulated by a series of post-translational (and intranuclear) modifications of DNA-interacting proteins, such as precursors to the sperm protamines. The amino acid composition of each sperm protamine is remarkably simple (lys + arg + gly ≥96 mol%). This system of spermiogenic/spermatozoal proteins in the neogastropod M. brandaris clearly differs from that in patellogastropods and archaeogastropods, and it may be helpful in understanding evolutionary changes in the chromatin condensation pattern during the spermiogenesis of gastropod molluscs. © 1994 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1059-910X
    Keywords: Ultrastructure ; Immunocytochemistry ; Chromatin structure ; Nuclear proteins ; Testis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: We have followed the fine structural distribution of two nucleosomal core histones, H2B and H3, and of protamines in the course of mouse spermiogenesis by means of specific antibodies and ultrastructural immunocytochemistry.Our results demonstrate that the nuclear labeling density of histone H2B decreases during steps 6-8 and then increases again in step 9-10 spermatids, while the labeling for histone H3 is constant throughout this period. In step 12 spermatids, the anti-H2B antibody labels mainly the central area of the nucleus. The first signs of protamine labeling are present in step 12 spermatids, where the gold grains can be found over the periphery of the nucleus. Later on, protamine labeling constantly increases and, by the end of spermiogenesis, the whole nucleus is labeled.We suggest that the morphological and structural differences between the central area and the periphery of mouse spermatids are, at least partly, due to a difference in the protein moiety associated with DNA. The central area, which is peculiar to the mouse and has been previously considered as a focus of chromatin condensation, represents, however, the last nuclear region containing histones and consequently the last area where the substitution of histones by protamines takes place.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 10 (1915), S. 53-65 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Additional Material: 3 Tab.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 8 (1992), S. 117-120 
    ISSN: 0749-503X
    Keywords: Thioredoxin ; TRX1 ; TRX2 ; genetic map location ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The two genes encoding thioredoxims in Saccharomyces cerevisiae, TRX1 and TRX2, map to chromosome XII and VII, respectively. From the DNA sequence of the intragenic region TRX1 is 500 bp downstream of PDC1. Tetrad analysis places TRX21·1 cM from ADE3, while a physical map of this region positions TRX2 4·5 kb downstreams of ADE3. The mapping of TRX1 adjacent to PDC1 clarifies previous results (Muller, E. G. D. J. Biol. Chem. 266, 9194-9202, 1991) that suggested a third thioredoxims gene.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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