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  • Chemistry  (6)
  • 1
    Electronic Resource
    Electronic Resource
    Surface phenomena in chemistry and biology. Edited by J. F. Danielli, K. G. A. Pankhurst, and A. C. Riddiford. Pergamon Press, New York, 1959. 330 pp. $10.00. (1959)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Polymer Science 40 (1959), S. 278-279 
    Details
    ISSN: 0022-3832
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pol.1959.1204013627
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Interaction of alcohols with proteins (1978)
    New York : Wiley-Blackwell
    Biopolymers 17 (1978), S. 2121-2131 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The kinetics of denaturation of egg albumin have been determined for methanol, ethanol, propanol, and butanol. The reactions are first order in respect to protein but between 11th and 18th order for the alcohols. The denaturation reaction is characterized by a large temperature coefficient with little or no dependence on pH. There is a marked change of pH when proteins are denatured. A series of eight proteins has been studied. There is surprisingly little difference in susceptibility to alcohol denaturation between the various proteins. Methanol, ethanol, propanol, and butanol are strongly bound to egg albumin - butanol being the most strongly bound. The binding of alcohol is probably accompanied by protein dehydration. The polyhydric alcohols' behavior is much different. These alcohols do not denature proteins and the protein is hydrated. Sucrose produces the greatest degree of hydration.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1978.360170907
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Stability of proteins in guanidine·HCl solutions (1975)
    New York : Wiley-Blackwell
    Biopolymers 14 (1975), S. 2197-2209 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A new method has been described for the study of the denaturation of proteins by guanidine·HCl. The pH of an unbuffered solution of protein is monitored as Gu·HCl solution at a constant rate is run into the protein solution. As the protein undergoes the transition from the native to denatured state a significant and fairly abrupt change in the pH is observed. The behaviour of 14 proteins has been explored. Lysozyme, pepsin, α-lactalbumin, lima bean trypsin inhibtor, and insulin failed to yield satisfactory transitions by this method. The method is entirely satisfactory with the other proteins. The maximum stabilities of the proteins in respect to Gu·HCl concentration and pH, and at zero rate (by extrapolation) of delivery of Gu·HCl have been studied. The relative stabilities of the proteins differ greatly. The stabilities are not related in a simple way to any known parameter.To supplement the pH change method outlined, the viscosities of nine proteins have been studied as a function of Gu·HCl concentration. A useful empirical equation relating the viscosity of a Gu·HCl solution to its molar concentration has been developed. The linear relationship between the relative fluidity and protein concentration has been confirmed and the intrinsic viscosities of the proteins have been calculated. The viscosities of the proteins vary significantly in respect to Gu·HCl concentration. All of the proteins undergo transitions from the native to the denatured state as shown by increases in the viscosities of their solutions. These transitions coincide closely with those found by the pH change method in respect to Gu·HCl concentration and pH. After the initial transition, the proteins continue to expand (viscosity increases) as the Gu·HCl concentration increases, indicating that the denatured state consists of many molecular configurations likely differing little in their energy content. The presence of disulfide bonds tends to limit the expansion of the protein molecules.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1975.360141015
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Solubilities of amino acids (1978)
    New York : Wiley-Blackwell
    Biopolymers 17 (1978), S. 1091-1100 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The Mettler/Paar precision density meter DMA-02D has been used to determine the concentration of saturated solutions of amino acids at 20.0, 25.0, and 29.8 °C. The technique has proven itself an elegant and precise method. The solubilities of all of the amino acids with the exceptions of proline, lysine, and cystine have been measured. The Gibbs free energies of transfer from saturated water solution to 1M Na2SO4 and to 1M Gu·HCL along with the van't Hoff heats and entropies have been calculated. The van't Hoff heats have been compared with the calorimetrically determined heats for some of the amino acids. The Lumry-Rajender relation between the entropy and heats has been observed. The process of transfer of the amino acids from water to the solvents is primarily enthalpic rather than entropic.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1978.360170421
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  • 5
    Electronic Resource
    Electronic Resource
    Temperature dependence of partial volumes of proteins (1973)
    New York : Wiley-Blackwell
    Biopolymers 12 (1973), S. 2351-2358 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The change of the apparent partial specific volumes of egg albumin, bovine serum albumin, bovine methemoglobin, β-lactoglobulin, and lysozyme with temperature through the thermal transitions of the proteins have been measured with dilatometers. Four regions in the plot of the apparent partial specific volumes against temperature can be recognized: (1) linear sections extending from 25°C up to 45-50°C: (2) a decrease in slope between 50°C and 60°C; (3) a sharp increase in slope with increasing temperature coinciding with the appearance of heat coagulation of the protein and followed by (4) a decrease in the slope. The return of the protein samples to 25°C yields linear relations between the apparent partial specific volumes of the heat-denatured proteins and the decreasing temperature.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1973.360121013
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Binding of water and electrolytes to proteins. An equilibrium dialysis study (1976)
    New York : Wiley-Blackwell
    Biopolymers 15 (1976), S. 1573-1583 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The technique of equilibrium dialysis has been used to study water and salt binding to egg albumin, to human carbon monoxide hemoglobin, and to bovine serum albumin. The salts used were CsCl, KCl, NaCl, LiCl, Gu·HCl, NaBr, Cs2SO4, K2SO4, Na2SO4, Li2SO4, and Gu2SO4. The amount of water bound by proteins depends on the probe being used. Sulfates tend to bind to proteins and they also increase the water binding. At saturation, about 41 and 140 mol Gu·HCl bind to 1 mol egg albumin and to 1 mol carbon monoxide hemoglobin, respectively. Both proteins are dehydrated by Gu·HCl.The hydrodynamic hydration of egg albumin as determined by viscosity appers to increase as the relative viscosity of the medium increases.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1976.360150811
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