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  • 1
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 154 (1944), S. 736-736 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] IN reply to the above communications, I wish to say that the main point in my complaint is that in two closely allied fields of chemistry the connecting link –CONH– is being called by two different names, namely, ‘amide’ and ‘peptide’, and that the expression ‘amide (or amido) group’ is being ...
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 154 (1944), S. 486-486 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] PROTEIN chemistry has its origins in physiology. For the last half-century the group formed by condensing the carboxyl group of an amino-acid with the amino group of another amino-acid has been called a peptide group, and the long molecule formed by condensing a number of amino-acids, a ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 138 (1936), S. 758-759 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] IN a theory put forward in these columns in March last1, it was suggested that the molecule of simple native protein may contain closed polypeptides : that the polypeptides, open or closed, fall into rings : and that the ring system is such as to allow the possibility of a ...
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 130 (1932), S. 24-25 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] THE swelling of protein gels and tissues under the influence of acid or alkali is due mainly to osmotic forces set up on account of salt formation between the protein and the acid or base. Osmotic swelling always shows two well-marked maxima, one in the acid and one in the alkaline range, and ...
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 132 (1933), S. 515-515 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A FEW years ago, one of us (T.M1,2) showed that by freezing, water could be withdrawn from a gelatin gel, the concentration of the remaining gel at equilibrium with any temperature increasing with falling temperature down to a temperature of −20°, below which no further water ...
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Fresenius' Zeitschrift für analytische Chemie 95 (1933), S. 365-371 
    ISSN: 1618-2650
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Colloid & polymer science 54 (1931), S. 46-49 
    ISSN: 1435-1536
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Zusammenfassung 1. Die Quellung gereinigter Gelatine, die in alkalischen Lösungen stattfindet (osmotische Quellung), ist unabhängig vom Volumen der Lösung, vorausgesetzt, daß die Temperatur tief genug ist, um eine hydrolytische Spaltung zu vermeiden (0° C). 2. Die Quellung der Gelatine in Salzlösungen ist innerhalb eines weiten Temperaturbereiches und innerhalb einer großen Salzkonzentration unabhängig vom Volumen der Lösung. Dies trifft zu, gleichgültig ob die Quellung ein Gleichgewicht erreicht, oder ob sie schließlich bis zur Auflösung führt.
    Type of Medium: Electronic Resource
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