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  • Wiley-Blackwell  (37)
  • American Association for the Advancement of Science  (27)
  • 1995-1999  (25)
  • 1980-1984  (23)
  • 1965-1969  (16)
Collection
Keywords
Publisher
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    The C-terminal extrahelical peptide of type I collagen and its role in fibrillogenesis in vitro: Effects of Ethylurea (1984)
    New York : Wiley-Blackwell
    Biopolymers 23 (1984), S. 313-323 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Ethylurea was used to weaken hydrophobic interactions during collagen fibrillogenesis in vitro. Intact and enzyme-digested type I collagen was studied. In all preparations, ethylurea decreased the extent and rate of fibril formation, inhibition being greatest in the enzyme-digested collagens. With intact collagen (and probably also with carboxypeptidasedigested collagen), there was no evidence the ethylurea altered the mechanism of fibril growth; in pepsin-digested collagen, however, the growth mechanism was altered by ethylurea, possibly reflecting a conformational change of the “hydrophobic cluster” in the C-terminal peptide. Such a structural change could occur in a hydrophobic environment once the distal portion of the C-terminal peptide (presumed to be essential for its structural stability) is removed by pepsin. The results further emphasize the importance of hydrophobic interactions in collagen fibril nucleation and growth in vitro.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360230210
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  • 2
    Electronic Resource
    Electronic Resource
    Surface aeration in a small, agitated, and sparged vessel (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 981-993 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: In a recent publication, a technique was outlined for measuring surface aeration rates in an agitated vessels while sparging, and it was shown that surface aeration rates fall rapidly with increasing sparge rates. That work was conducted in a 0.61 m diam vessels. The work reported here was done in a small vessel (0.22 m diam) where surface aeration has been reported to be of particular significance. In general, the results obtained in the small vessel confirmed those in the large one and in addition were generally in good agreement with those recently published elsewhere for an almost identical geometry. For typical practical power inputs and sparge rates, the rate of surface aeration was never more than 20% of the sparge rate and generally less than 5%. These results indicate that surface aeration is of considerably less importance than has generally been believed following the findings of workers who estimated its effect by comparing KLa values under unsparged conditions with those when sparging.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220507
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  • 3
    Electronic Resource
    Electronic Resource
    Bacterial degradation of aromatic compounds (1967)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 9 (1967), S. 33-44 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The bacterial degradation of catechol, 3-methylcatechol, 2,3-dihydroxy-β-phenylpropionic acid, and protocatechuic acid has been studied in detail. From the results obtained a general sequence has been proposed for the microbial oxidation of dihydroxy aromatic compounds.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260090105
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  • 4
    Electronic Resource
    Electronic Resource
    Virial coefficients, Kihara and Lennard-Jones parameters for methyl borate (1965)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 11 (1965), S. 365-366 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690110232
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  • 5
    Electronic Resource
    Electronic Resource
    The viscosity of liquid metals (1966)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 12 (1966), S. 395-400 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: In order to make the kinetic theory of liquid viscosity tractable, an approximate from is suggested for the perturbation of the radial distribution function of a monatomic liquid by a nonuniform flow field. Substitution of this form into the microscopic expression for the pressure tensor yields an equation for liquid viscosity in terms of the equilibrium distribution function and the interatomic potential energy function. This equation establishes the basis for a corresponding states correlation of the viscosity of liquid metals based on atomic parameters.The viscosity data for twenty-one molten metals are made to fall on a single curve by the adjustment of one microscopic parameter. It is found that this empirically determined parameter has the proper fundamental significance. Therefore it is possible to estimate it independently and to use the general correlation for estimating the viscosity of a metal for which data are not available. Also it is suggested that the atomic parameters determined from viscosity data in this way might be used to correlate other properties of the liquid metals.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690120233
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  • 6
    Electronic Resource
    Electronic Resource
    Structural Characteristics of the Short-Tail Fibers of T4 Bacteriophage (1982)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 18 (1982), S. 363-375 
    Details
    ISSN: 0730-2312
    Keywords: T4 bacteriophage ; short-tail fibers ; fiber formation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The characteristics of pure preparations of short-tail fibers of bacteriophage T4 have been studied in the optical and electron microscope. Three main structures were observed: 1) spheres of 8.1 nm diameter; 2) fibers 43 nm long and 3.8 nm thick; and 3) fibers 54 nm long and 3.2 nm thick. Both types of fibers exhibited a regular beaded appearance. The 43-nm fibers were the most abundant structure. During the process of purification of the short-tail fibers, the formation of aggregates was observed each time the material containing the short-tail fibers was dialyzed against saline solutions. These aggregates became increasingly fibrous (as observed in the optical microscope) as the material used was increasingly enriched in short-tail fibers. Finally, most of the aggregates were of the fibrous type when they were formed from a purified preparation of short-tail fibers. In the electron microscope, it was found that the filamentous aggregates were organized in well-defined bundles. The amino acid composition of the highly purified short-tail fibers was also determined. Among the known fibrous proteins, the ones that most resemble the amino acid composition of the short-tail fibers are actin and fibrinogen. These observations are discussed in relation to the T4 short-tail fiber structure and their localization on the hexagonal baseplate of the T4 tail structure.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.1982.240180309
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  • 7
    Electronic Resource
    Electronic Resource
    Volume changes accompanying the thermal denaturation of deoxyribonucleic acid. I. Denaturation at neutral pH (1969)
    New York : Wiley-Blackwell
    Biopolymers 7 (1969), S. 527-537 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Dilatometric measurements were made to determine the change in apparent specific volume ϕ of DNA resulting from thermal denaturation in neutral solution, ϕ increased continuously with temperature in the range 10-85°C. No deviations from a monotonically rising curve were observed in the ϕ versus temperature profile in the region of the melting temperature. The results are interpreted in terms of a partial loss of the preferentially bound DNA hydration shell. The nature of the well known buoyant density difference between native and denatured DNA was investigated by evaluating the densities in a series of cesium salt gradients at constant temperature. Extrapolation of the results to zero water activity indicates that the partial specific volumes of anhydrous native and denatured DNA are equal. The density difference at nonzero water activities is attributed to decreased hydration in the denatured state. The absence of a related change in ϕ accompanying the denaturation in the dilatometric experiments suggests that the probable volume change associated with loss of bound water during denaturation is accompanied by other compensatory volume effects. The possible nature of these volume effects is discussed.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1969.360070410
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  • 8
    Electronic Resource
    Electronic Resource
    The C-terminal extrahelical peptide of type I collagen and its role in fibrillogenesis in vitro (1982)
    New York : Wiley-Blackwell
    Biopolymers 21 (1982), S. 2291-2313 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The formation in vitro of fibrils from type I acid-soluble calf skin collagen has been studied before and after removal of the extrahelical peptides with carboxypeptidase and with pepsin. Turbidimetric studies show that the mechanism of fibril growth in undigested collagen is similar to that in pepsin-digested collagen; following carboxypeptidase digestion, however, a different growth mechanism was apparent. The two mechanisms have been further characterized by electron microscopy. In the course of formation of fibrils from undigested collagen, “early fibrils” (short D-periodic fibrils that have both ends visible) occurred in the lag phase under the precipitating conditions employed here. After pepsin or carboxypeptidase digestion of the collagen no “early fibrils” were seen. In carboxypeptidase-digested collagen, lateral assembly was inhibited; after pepsin digestion, linear assembly was inhibited. Complete removal of the extrahelical peptides prevented fibril formation under the conditions used here. Electron-optical examination of segment-long-spacing (SLS) dimers established a more complete removal of the C-terminal peptide after carboxypeptidase digestion than after pepsin digestion. Analyses of staining patterns of SLS dimers and fibrils from undigested and digested samples showed that the C-terminal peptide in SLS crystallites and fibrils formed from undigested collagen is in a condensed conformation. A proposed conformation, in which condensation occurs predominantly in a hydrophobic region at the proximal end of the C-terminal peptide, is discussed in terms of a dual role for the C-terminal peptide in fibrillogenesis. One role, shared with the N-terminal peptide, is to participate in interactions between the 4D-staggered molecules leading to the formation of linear aggregates; the other is to participate in interactions between these linear aggregates giving rise to D-periodic aggregates and lateral (as well as linear) growth.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360211115
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  • 9
    Electronic Resource
    Electronic Resource
    The conformational analysis of peptides using fourier transform IR spectroscopy (1995)
    New York : Wiley-Blackwell
    Biopolymers 37 (1995), S. 251-263 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Fourier transform infrared spectroscopy (FTIR) can be used for conformational analysis of peptides in a wide range of environments. Measurements can be performed in aqueous solution, organic solvents, detergent micelles as well as in phospholipid membranes. Information on the secondary structure of peptides can be derived from the analysis of the strong amide I band. Orientation of secondary structural elements within a lipid bilayer matrix can be determined by means of polarized attenuated total reflectance-FTIR spectroscopy. Hydrogen-deuterium exchange can be monitored by the analysis of the, amide II band. This review gives some example of peptide systems studied by FTIR spectroscopy. Studies on alamethicin and α-aminoisobutyric acid containing peptides have shown that FTIR spectroscopy is a sensitive tool for identifying 310-helical structures. Changes in the structure of the magainins upon interaction with charged lipids were detected using FTIR spectroscopy. Tachyplesin is an example of a β-sheet containing membrane active peptide. Polarized ir spectroscopy reveals that the antiparallel β-sheet structures of tachyplesin are oriented parallel to the membrane surface. Synthesis of peptides corresponding to functionally/structurally important regions of large proteins is becoming increasingly popular. FTIR spectroscopy has been used to analyze the structure of synthetic peptides corresponding to the ion-selective pore of the voltage-gated potassium channel. In biomembrane systems these peptides adopt a highly helical structure. Under conditions, where these peptides are aggregated the presence of some intermolecular β-sheet structure can also be detected. © 1994 John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360370404
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  • 10
    Electronic Resource
    Electronic Resource
    Styrene and isoprene friction factors in styrene-isoprene matrices (1998)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part B: Polymer Physics 36 (1998), S. 3079-3086 
    Details
    ISSN: 0887-6266
    Keywords: diffusion ; block copolymer ; monomeric friction factor ; Physics ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Monomeric friction factors, Ξ, for polystyrene (PS), polyisoprene (PI), and a polystyrene-polyisoprene (SI) diblock copolymer have been determined as a function of temperature in four poly(styrene-b-isoprene-b-styrene-b-isoprene) tetrablock copolymer matrices. The Rouse model has been used to calculate the friction factors from tracer diffusion coefficients measured by forced Rayleigh scattering. Within the experimental temperature range the tetrablock copolymers are disordered, allowing for measurement of the diffusion coefficient in matrices with average compositions determined by the tetrablock copolymers (23, 42, 60, and 80% styrene by volume). Remarkably, for a given matrix composition the styrene and isoprene friction factors are essentially equivalent. Furthermore, at a constant interval from the system glass transition temperature, Tg, all of the friction factors (obtained from homopolymer, diblock copolymer, and tetrablock copolymer dynamics) agree to within an order of magnitude. This is in marked contrast to results for miscible polymer blends, where the individual components generally have distinct composition dependences and magnitudes at constant T - Tg. The homopolymer friction factors in the tetrablock matrices were systematically slightly higher than those of the diblock, which in turn were slightly higher than those of the homopolymers in their respective melts, when all compared at constant T - Tg. This is attributed to the local spatial distribution of styrene and isoprene segments in the tetrablocks, which presents a nonuniform free energy surface to the tracer molecules. © 1998 John Wiley & Sons, Inc. J Polym Sci B: Polym Phys 36: 3079-3086, 1998
    Additional Material: 7 Ill.
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