Eggerer h (15 resultados)

Condición: New. In English.

gebundene Ausgabe. Condición: Gut. 216 Seiten Der Erhaltungszustand des hier angebotenen Werks ist trotz seiner Bibliotheksnutzung sehr sauber und kann entsprechende Merkmale aufweisen (Rückenschild, Instituts-Stempel.). In ENGLISCHER Sprache. Sprache: Englisch Gewicht in Gramm: 545.

Condición: New.

Condición: New. pp. 232.

Paperback. Condición: Brand New. reprint edition. 232 pages. 9.61x6.69x0.55 inches. In Stock.

Taschenbuch. Condición: Neu. Druck auf Anfrage Neuware - Printed after ordering - Enzymes perform the executive role in growth, energy conversion, and repair of a living organism. Their activity is adjusted to their en vironment within the cell, being turned off, switched on, or finely tuned by specific metabolites according to demands at the physiologi cal level. Each enzyme discovered in the long history of enzymology has revealed its own individuality. Even closely related members of a family differ in specificity, stability or regulatory properties. Despite these, at first sight overwhelming aspects of individuality, common factors of enzymic reactions have been recognized. Enzymes are stereospecific catalysts even when a nonspecific process would yield the same product. Knowledge of the detailed stereochemistry of an enzymic reaction helps to deduce reaction mechanisms and to ob tain insight into the specific binding of substrates at the active site. This binding close to catalytically competent groups is related to the enormous speed of enzyme-catalyzed reactions. The physical ba sis of rate-enhancement is understood in principle and further exploit ed in the design of small organic receptor molecules as model enzymes. These aspects of enzyme catalysis are discussed in Session 1. Session 2 emphasizes the dynamic aspects of enzyme substrate inter action. Substrate must diffuse from solution space to the enzyme's surface. This process is influenced and can be greatly facilitated by certain electrostatic propterties of enzymes. The dynamic events during catalysis are studied by relaxation kinetics or NMR techniques.…

Paperback. Condición: Like New. LIKE NEW. SHIPS FROM MULTIPLE LOCATIONS. book.

Condición: gut. 1981. Structural and Functional Aspects of Enzyme Catalysis: 32. Colloquium, 23. - 25. April 1981 Colloquium der Gesellschaft für Biologische Chemie in Mosbach Baden, 32 In deutscher Sprache. pages.

Paperback. Condición: Brand New. 3rd edition. 396 pages. German language. 7.90x5.20x0.90 inches. In Stock.

[28] pp.; 21.7 x 13.9 cm.; staple bound; black-and-white; edition size unknown; unsigned and unnumbered; offset-printed Periodical / zine published in conjunction with Amy Sillman exhibition titled "Transformer - or, how many lightbulbs does it take to change a painting?" held at Sikkema Jenkins Gallery, April 15 - May 15, 2010. Includes reproductions of work by Amy Sillman, Velimir Khlebnikov, Dieter Roth, Charles Peirce, Mike Smith, Picasso, Jasper Johns, Philip Guston, George Grosz, R.H. Quaytman, David Salle, Lisa Milroy, Claes Oldenburg, James Rosenquist, Palmer Hayden, Francis Picabia, George Clinton / P-Funk, and Christina Ramberg. Second printing does not include the Audio CD that was included in the first printing. Fine. As issued. Does not include folded poster, it is unclear if the second edition included the folder poster or not.…

Condición: new. Questo è un articolo print on demand.

Taschenbuch. Condición: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -Enzymes perform the executive role in growth, energy conversion, and repair of a living organism. Their activity is adjusted to their en vironment within the cell, being turned off, switched on, or finely tuned by specific metabolites according to demands at the physiologi cal level. Each enzyme discovered in the long history of enzymology has revealed its own individuality. Even closely related members of a family differ in specificity, stability or regulatory properties. Despite these, at first sight overwhelming aspects of individuality, common factors of enzymic reactions have been recognized. Enzymes are stereospecific catalysts even when a nonspecific process would yield the same product. Knowledge of the detailed stereochemistry of an enzymic reaction helps to deduce reaction mechanisms and to ob tain insight into the specific binding of substrates at the active site. This binding close to catalytically competent groups is related to the enormous speed of enzyme-catalyzed reactions. The physical ba sis of rate-enhancement is understood in principle and further exploit ed in the design of small organic receptor molecules as model enzymes. These aspects of enzyme catalysis are discussed in Session 1. Session 2 emphasizes the dynamic aspects of enzyme substrate inter action. Substrate must diffuse from solution space to the enzyme's surface. This process is influenced and can be greatly facilitated by certain electrostatic propterties of enzymes. The dynamic events during catalysis are studied by relaxation kinetics or NMR techniques. 232 pp. Englisch.…

Condición: New. Print on Demand pp. 232 116 Figures, 67:B&W 6.69 x 9.61 in or 244 x 170 mm (Pinched Crown) Perfect Bound on White w/Gloss Lam.

Condición: New. PRINT ON DEMAND pp. 232.

Taschenbuch. Condición: Neu. This item is printed on demand - Print on Demand Titel. Neuware -Enzymes perform the executive role in growth, energy conversion, and repair of a living organism. Their activity is adjusted to their en vironment within the cell, being turned off, switched on, or finely tuned by specific metabolites according to demands at the physiologi cal level. Each enzyme discovered in the long history of enzymology has revealed its own individuality. Even closely related members of a family differ in specificity, stability or regulatory properties. Despite these, at first sight overwhelming aspects of individuality, common factors of enzymic reactions have been recognized. Enzymes are stereospecific catalysts even when a nonspecific process would yield the same product. Knowledge of the detailed stereochemistry of an enzymic reaction helps to deduce reaction mechanisms and to ob tain insight into the specific binding of substrates at the active site. This binding close to catalytically competent groups is related to the enormous speed of enzyme-catalyzed reactions. The physical ba sis of rate-enhancement is understood in principle and further exploit ed in the design of small organic receptor molecules as model enzymes. These aspects of enzyme catalysis are discussed in Session 1. Session 2 emphasizes the dynamic aspects of enzyme substrate inter action. Substrate must diffuse from solution space to the enzyme's surface. This process is influenced and can be greatly facilitated by certain electrostatic propterties of enzymes. The dynamic events during catalysis are studied by relaxation kinetics or NMR techniques.Springer-Verlag KG, Sachsenplatz 4-6, 1201 Wien 232 pp. Englisch.…