kretsinger robert (15 Ergebnisse)

Zustand: Good. Former library book; may include library markings. Used book that is in clean, average condition without any missing pages.

hardcover. 1st. 8vo, 351 pp. Fine copy (issued without dust jacket).

Hardcover. Zustand: Very Good+. No Jacket. 1st Ed. 351pp, octavo hardcover in glossy boards. covers clean and sharp, strong binding, interior text clean.

Zustand: New. pp. 240.

Zustand: New. This is a Brand-new US Edition. This Item may be shipped from US or any other country as we have multiple locations worldwide.

Zustand: New. This is a Brand-new US Edition. This Item may be shipped from US or any other country as we have multiple locations worldwide.

Zustand: Used. pp. 240.

Paperback. Zustand: Brand New. 240 pages. 9.00x6.25x0.75 inches. In Stock.

Zustand: Used. pp. 240.

Zustand: Hervorragend. Zustand: Hervorragend | Seiten: 316 | Sprache: Englisch | Produktart: Bücher | We characterize eight families of Leucine Rich Repeat (LRR) units in terms of their amino acid sequences and their tertiary structures. Tandem LRRs form helices with a broad range of parameters. These LRR helices have a broad range of functions in eukaryotes, prokaryotes, and viruses. We explore the relationships of these structures to the functions of the LRR proteins and consider their evolution(s).

Zustand: Sehr gut. Zustand: Sehr gut | Seiten: 316 | Sprache: Englisch | Produktart: Bücher | We characterize eight families of Leucine Rich Repeat (LRR) units in terms of their amino acid sequences and their tertiary structures. Tandem LRRs form helices with a broad range of parameters. These LRR helices have a broad range of functions in eukaryotes, prokaryotes, and viruses. We explore the relationships of these structures to the functions of the LRR proteins and consider their evolution(s).

Hardcover. Zustand: Brand New. 351 pages. 9.00x6.00x0.75 inches. In Stock.

Hardcover. Zustand: Brand New. 1st edition. 581 pages. 9.40x6.20x1.50 inches. In Stock.

Zustand: Gut. Zustand: Gut | Seiten: 2812 | Sprache: Englisch | Produktart: Bücher | In biochemistry, a metalloprotein is a generic term for a protein that contains a metal cofactor. The metal may be an isolated ion or may be coordinated with a nonprotein organic compound, such as the porphyrin found in hemoproteins. In some cases, the metal is co-coordinated with a side chain of the protein and an inorganic nonmetallic ion. This kind of protein-metal-nonmetal structure is seen in iron-sulfur clusters Metalloproteins deals with all aspects related to the intracellular and extracellular metal-binding proteins, including their structures, properties and functions. The biological roles of metal cations and metal-binding proteins are endless. They are involved in all crucial cellular activities. Many pathological conditions are related to the problematic metal metabolism. Research in metalloprotein-related topics is therefore rapidly growing, and different aspects of metal-binding proteins progressively enter curricula at Universities andeven at the High School level on occasion. However, no key resource providing basic, but comprehensible knowledge on this rapidly expanding field exists. The Encyclopedia of Metalloproteins aims to bridge this gap, and will attempt to cover various aspects of metalloprotein/metalloproteomics and will deal with the different issues related to the intracellular and extracellular metal-binding proteins, including their structures, properties and functions. The goal is to cover exhaustively all catalytically and biologically crucial metal ions and to find at least one interacting protein for other metal ions. The Encyclopedia of Metalloproteins will provide a key resource for advanced undergraduate and graduate students, researchers, instructors, and professors interested in protein science, biochemistry, cell biology, and genetics.

Buch. Zustand: Neu. Druck auf Anfrage Neuware - Printed after ordering - In biochemistry, a metalloprotein is a generic term for a protein that contains a metal cofactor. The metal may be an isolated ion or may be coordinated with a nonprotein organic compound, such as the porphyrin found in hemoproteins. In some cases, the metal is co-coordinated with a side chain of the protein and an inorganic nonmetallic ion. This kind of protein-metal-nonmetal structure is seen in iron-sulfur clustersMetalloproteins deals with all aspects related to the intracellular and extracellular metal-binding proteins, including their structures, properties and functions. The biological roles of metal cations and metal-binding proteins are endless. They are involved in all crucial cellular activities. Many pathological conditions are related to the problematic metal metabolism. Research in metalloprotein-related topics is therefore rapidly growing, and different aspects of metal-binding proteins progressively enter curricula at Universities andeven at the High School level on occasion. However, no key resource providing basic, but comprehensible knowledge on this rapidly expanding field exists. The Encyclopedia of Metalloproteins aims to bridge this gap, and will attempt to cover various aspects of metalloprotein/metalloproteomics and will deal with the different issues related to the intracellular and extracellular metal-binding proteins, including their structures, properties and functions. The goal is to cover exhaustively all catalytically and biologically crucial metal ions and to find at least one interacting protein for other metal ions. The Encyclopedia of Metalloproteins will provide a key resource for advanced undergraduate and graduate students, researchers, instructors, and professors interested in protein science, biochemistry, cell biology, and genetics.