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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 31 (1992), S. 8810-8815 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 31 (1992), S. 12701-12705 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 280 (1979), S. 693-696 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1 Relaxation spectrum of an abstract protein (solid line) and that of a random coil polypeptide (dotted line). There are two experimental approaches to a quantitative determination of protein stability: the first is based on the study of peptide hydrogen exchange in native protein and the ...
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of solution chemistry 18 (1989), S. 927-936 
    ISSN: 1572-8927
    Keywords: Microcalorimetry ; alcohols ; aqueous solution ; partial volume ; partial heat capacity ; hydration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Using a precise technique of scanning microcalorimetry the heat capacity differences between water and dilute aqueous solutions of ethanol, n-propanol, n-butanol and n-pentanol were measured from 5 to 125°C and the partial molar heat capacities of these substances in water were determined. It was found that the heat capacity increment for alcohol disolved in water is proportional to the number of the-CH 2 − groups and decrease with a temperature increase. The heat capacity increment of hydration of non-polar groups is shown to be positive and large at room temperature and decreases in magnitude as the temperature increases. In contrast, the heat capacity increment of hydration of polar groups is negative at room tempreature and increases as the temperature increases. From the temperature dependence of the heat capacity increment one can assume that the water molecules solvated by the non-polar groups of the alcohols behave in a non-cooperative manner.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Journal of structural chemistry 9 (1968), S. 5-7 
    ISSN: 1573-8779
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The partial molar volumes of various compounds that model protein constituent groups, such as tripeptides (Gly-X-Gly, where X = Gly, Ala, Val, Leu, Ile, Pro, Met, His, Ser), homopeptides (Glyn, n = 3, 4, 5), and simple organic analogues of amino acid side chains (methanol, acetamide, propanamide, acetic acid, propanoic acid, n-butanamine, n-butanamine nitrate, n-propylguanidine nitrate, 4-methylphenol), have been determined in aqueous solution with a vibrational densimeter in the temperature range of 5-85°C. The partial molar volumes of amino acid side chains and the peptide unit were estimated from the data obtained. Assuming additivity of component groups, the partial molar volumes of polypeptide chains of several proteins over a broad temperature range were calculated. The partial molar volume functions of four proteins (myoglobin, cytochrome C, ribonuclease A, lysozyme) were compared with those determined experimentally for the unfolded and native forms of these proteins. It has been shown that the average deviation of the calculated functions from the experimental ones does not exceed 3% over the temperature range studied.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 22 (1983), S. 113-118 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Denatured histones H1 and H5 can be readily refolded on salt addition. Their digestion by trypsin leads to limit peptides of about 80 residues having the same nmr and CD spectra as those of the intact parent histones. Scanning microcalorimetry shows that (1) the folded structures of H1 and H5 are located entirely in their limit peptides; (2) both have values of the specific denaturation enthalpy typical for small globular proteins; and that (3) both exhibit a classic “2-state” transition (ΔHdcal = ΔHdvan't Hoff). The heat-denaturation profiles of H5 measured using intrinsic and extrinsic Cotton effect and side-chain nmr peaks do not coincide at all. Only the intrinsic Cotton effects give a Tm and ΔHdvan't Hoff close to that from microcalorimetry. We conclude that these proteins exhibit large-scale side-chain motions that precede the macroscopic cooperative transition.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 8 (1969), S. 559-571 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The possibility of determining the free energy of stabilization ΔG0 of native DNA structure with the help of calorimetric data on heats ΔH of transition from the native to denaturated state is considered. Results of microcalorimetric measurements of heats of denaturation of T2 phage DNA at, different values of pH and ionic strength of solution are given. Values of free energy of stabilization of the DNA native structure ΔG0 under various conditions have been obtained. It is shown that under conditions close to physiological ΔG0 approaches 1200 cal/mole per base pair.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 9 (1970), S. 127-139 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Effects of heat in heated solution of tropocollagens of different origins were calorimetrically studied. It was found that denaturation enthalpy and entropy of different tropocollagens increase with increasing imino acid content and thermostability. It is shown that the value and dependence of denaturational enthalpy and entropy on the denaturation temperature for tropocollagens with different imino acid contents are inconsistent with the assumption that the native structure of tropocollagen is stabilized only by intramolecular hydrogen bonds. A supposition is made that the regular water structure near the macromolecule plays an essential role in stabilizing the structure. From the character of tropocollagen melting curves in salt-free solution it is found that the tropocollagen macromolecule is linearly heterogeneous. It is shown that the complex pattern of thermal absorption observed in tropocollagen salt, solution is connected with pre-denaturational conformational transformation when approaching conditions close to the physiological.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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