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  • 1985-1989  (3)
  • 1
    Online Resource
    Online Resource
    Berlin, Heidelberg :Springer Berlin / Heidelberg,
    Keywords: Thermodynamics. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (462 pages)
    Edition: 1st ed.
    ISBN: 9783642711145
    Language: English
    Note: Intro -- Thermodynamic Data for Biochemistry and Biotechnology -- Copyright -- Preface -- Contents -- Addresses of Authors and Referees -- Section I Introduction -- Chapter 1 Present and Future Uses and a Bit of History -- Section II Nonreacting Systems -- Chapter 2 Partial Molar Volumes of Biochemical Model Compounds in Aqueous Solution -- Chapter 3 Specific Volumes of Biological Macromolecules and Some Other Molecules of Biological Interest -- Chapter 4 Partial Molar Compressibilities of Organic Solutes in Water -- Chapter 5 Heat Capacities of Biological Macromolecules -- Chapter 6 Thermodynamics of Carbohydrate Monomers and Polymers in Aqueous Solution -- Section III Interactions in Solution -- Chapter 7 Thermodynamic Data for Protein-Ligand Interaction -- Chapter 8 Thermodynamics of Protein-Protein Association -- Chapter 9 Hemoglobin -- Chapter 10 Gas-Liquid and Solid-Liquid Phase Equilibria in Binary Aqueous Systems of Nonelectrolytes -- Chapter 11 Thermodynamic Parameters of Biopolymer-Water Systems -- Section V Phase Changes -- Chapter 12 The Formation of Micelles -- Chapter 13 Unfolding of Proteins -- Chapter 14 The Thermodynamics of Conformation Transitions in Polynucleotides -- Chapter 15 Methods for Obtaining Thermodynamic Data on Oligonucleotide Transitions -- Section VI Enzyme Catalyzed Processes -- Chapter 16 Thermodynamics of Enzymatic Reactions -- Subject Index.
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 26 (1987), S. 3544-3551 
    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
    Springer
    Journal of thermal analysis and calorimetry 35 (1989), S. 639-657 
    ISSN: 1572-8943
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Zusammenfassung Eine charakteristische Eigenschaft von Proteinen ist die marginale Stabilität der Sekundär- und Tertiärstrukturen. Deshalb ist es möglich, durch Austausch einzelner Aminosäuren messbare Stabilitätsänderungen hervorzurufen. Eine der besten Methoden zur Bestimmung der thermodynamischen Stabilitätsparameter ist die Wärmekapazitätsmikrokalorimetrie. Im vorliegenden Artikel werden die methodischen Grundlagen dieses Messverfahrens kurz beschrieben. Das Hauptgewicht liegt jedoch auf der Bestimmung der Beiträge der kovalenten und nicht-kovalenten Wechselwirkungen zur Gesamtstabilität von Proteinen. Am Beispiel von zwei biochemisch und biophysikalisch gut charakterisierten Proteinen, dem pankreatischen Trypsin Inhibitor /BPTI/ und /ROP/, werden die Grundideen der Separation der energetischen Einzelbeitäge diskutiert.
    Abstract: Резюме Протеины характериз уются незначительно й устойчивостью вторичной и третично й структуры, что делае т их чувствительны$ ми к возмущениям, вызв анными обменом тольк о одной аминокисло$ ты. Одним из оамых лучш их методов определен ия типичных пара$ метров их термодинам ической устойчивост и является высокочув$ ствительная сканиру ющая микрокалоримет рия. В статье описывают$ ся некоторые основны е методологические а спекты этого метода. Однако, главное внима ние уделено количеот венному определению ковалентных и некова лентных вкладов в общ ую стабильность про$ теинов. Общее логичес кое обоснование этог о метода показано на примере двух хорошо и зученных протеинов: и нгибитор трипсина BPTI в ROP.
    Notes: Abstract Proteins are characterized by a marginal stability of their secondary and tertiary structure that renders them susceptible to stability perturbations by single amino acid exchanges. One of the most powerful techniques to determine the typical thermodynamic stability parameters is high sensitivity scanning microcalorimetry. The present paper describes some basic methodological aspects of the technique. Main attention is, however, focussed on the determination and magnitude of covalent and noncovalent contributions to overall protein stability. Two well defined proteins, bovine pancreatic trypsin inhibitor /BPTI/ and /ROP/ have served to exemplify the general rationale of the approach.
    Type of Medium: Electronic Resource
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