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  • 1
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    Heidelberg : Spektrum Akademischer Verlag
    Call number: QR181:56(7)/korr.Nachdr. ; G181:2
    Keywords: Immune System / physiology ; Immune System / physiopathology ; Immunity ; Immunotherapy
    Notes: Translation of: Janeway's immunobiology.7th ed. 2008.
    Pages: xxvi, 1093 p. : ill.
    Edition: 7. Auflage, korr. Nachdruck
    ISBN: 9783662442272
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  • 2
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    Heidelberg : Spektrum Akademischer Verlag
    Call number: QR181:55(7)a
    Keywords: Immune System / physiology ; Immune System / physiopathology ; Immunity ; Immunotherapy
    Notes: Translation of: Janeway's immunobiology.7th ed. 2008.
    Pages: xxvi, 1093 p. : ill.
    Edition: 7. Auflage
    ISBN: 978-3-8274-2047-3
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  • 3
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    Berlin : Spektrum Spektrum
    Call number: QR181:55(9)
    Keywords: Immune System / physiology ; Immune System / physiopathology ; Immunity ; Immunotherapy
    Notes: Translation of: Janeway's immunobiology. 9th ed. 2018.
    Pages: xl, 1205 p. : ill.
    Edition: 9. Auflage
    ISBN: 978-3-662-56003-7
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  • 4
    Call number: C050:62 ; D015:11 ; D090:31 ; D110:5 ; F100:26 ; G100:31
    Keywords: Immunology ; Immune System / physiology ; Immune System / physiopathology ; Immunity ; Immunotherapy
    Notes: Prev. ed.: Immunobiology / Charles A. Janeway, Jr. ... [et al.].
    Pages: xix, 868 p. : ill. (chiefly col.)
    Edition: 8th ed.
    ISBN: 9780815342434
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    D090:31 departmental collection or stack – please contact the library
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  • 5
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    New York : Garland Science
    Call number: B086:42 ; F030:4
    Keywords: Immunology ; Immune System / physiology ; Immune System / physiopathology ; Immunity ; Immunotherapy
    Description / Table of Contents: Basic concepts in immunology -- Innate immunity -- Antigen recognition by B-cell and T-cell receptors -- The generation of lymphocyte antigen receptors -- Antigen presentation to T lymphocytes -- Signaling through immune system receptors -- The development and survival of lymphocytes -- T cell-mediated immunity -- The humoral immune response -- Dynamics of adaptive immunity -- The mucosal immune system -- Failures of host defense mechanism -- Allergy and hypersensitivity -- Autoimmunity and transplantation -- Manipulation of the immune response -- Evolution of the immune system
    Notes: Prev. ed.: Immunobiology / Charles A. Janeway, Jr. ... [et al.].
    Pages: xxi, 887 p. : ill. (chiefly col.) 1 CD-ROM (4 3/4 in.)
    Edition: 7th ed.
    ISBN: 9780815341239
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  • 6
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 0887-3585
    Keywords: thermodynamics ; calorimetry ; protein-hormone interaction ; drug design ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The ability to predict the strength of the association of peptide hormones or other ligands with their protein receptors is of fundamental importance in the fields of protein engineering and rational drug design. To form a tight complex between a flexible peptide hormone and its receptor, the large loss of configurational entropy must be overcome. Recently, the crystallographic structure of the complex between angiotensin II and the Fab fragment of a high affinity monoclonal antibody has been determined (Garcia, K. C., Ronco, P. M., Verroust, P. J., Brünger, A. T., Amzel, L. M. Three-dimensional structure of an angiotensin II-Fab complex at 3 Å: Hormone recognition by an anti-idiotypic antibody. Science 257:502-507, 1992). In this paper we present a study of the thermodynamics of the association by high sensitivity isothermal titration calorimetry. The results of the experiments indicate that at 30°C the binding is characterized by (1) a ΔH of -8.9 ± 0.7 kcal mol-1, (2) a ΔCp of -240 ± 20 cal K-1 mol-1, and (3) the release of 1.1 ± 0.1 protons per binding site in the pH range 6.0-7.3. Using these values and the previously determined binding constant in phosphate buffer, ΔG at 30°C is estimated as -11 kcal mol-1 and ΔS as 6.9 cal K-1 mol-1. The calorimetric data indicate that binding is favored both enthalpically and entropically. These results have been complemented by structural thermodynamic calculations. The calculated and experimentally determined thermodynamic quantities are in good agreement. Entropically, the loss of configurational entropy is more than compensated by the entropy gain from solvent release associated with the hydrophobic effect. Enthalpically, binding is favored by polar interactions (hydrogen bonding). Consequently, the problem of binding flexible hormones is solved in much the same way as the folding of an unstructured polypeptide chain into a globular protein. © 1993 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 0887-3585
    Keywords: entropy ; thermodynamics ; binding energetics ; translational entropy ; macromolecular interactions ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The loss of translational degrees of freedom makes an important, unfavorable contribution to the free energy of binding. Examination of experimental values suggest that calculation of this entropy using the Sackur-Tetrode equation produces largely overestimated values. Better agreement is obtained using the cratic entropy. Theoretical considerations suggest that the volumes available for the movement of a ligand in solution and in a complex are rather similar, suggesting also that the cratic entropy provides the best estimate of the loss of translational entropy. © 1994 John Wiley & Sons, Inc.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 0887-3585
    Keywords: calorimetry ; desolvation ; linear extrapolation model ; binding ; denaturation ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The effects of urea on protein stability have been studied using a model system in which we have determined the energetics of dissolution of a homologous series of cyclic dipeptides into aqueous urea solutions of varying concentration at 25°C using calorimetry. The data support a model in which urea denatures proteins by decreasing the hydrophobic effect and by directly binding to the amide units via hydrogen bonds. The data indicate also that the enthalpy of amide hydrogen bond formation in water is considerably higher than previously estimated. Previous estimates included the contribution of hydrophobic transfer of the α-carbon resulting in an overestimate of the binding between urea and the amide unit of the backbone and an underestimate of the binding enthalpy. Proteins 31:107-115, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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