Evolution protein structure function (33 résultats)

Etat : Gut. 501 pages Innen sauberer, guter Zustand. Hardcover, Pappeinband, mit den üblichen Bibliotheks-Markierungen, Stempeln und Einträgen, innen wie außen, siehe Bilder. (Evtl. auch Kleber- und/oder Etikettenreste, sowie -abdrücke durch abgelöste Bibliotheksschilder). B10-01-04P|[X2932] Sprache: Englisch Gewicht in Gramm: 1172. …

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Paperback. Etat : Brand New. 237 pages. 9.25x7.25x0.50 inches. In Stock.

Hardcover. Etat : Good+. No Dust Jacket. First Edition; First Printing. UCLA Forum In Medical Sciences; 350 pages; graphs. Ex-Library copy with usual identifiers. Light rubbing on the covers. Good condition otherwise. No other noteworthy defects. No markings on text pages. ; Your satisfaction is our priority. We offer free returns and respond promptly to all inquiries. Your item will be carefully cushioned in bubble wrap and securely boxed. All orders ship on the same or next business day. Buy with confidence.…

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Etat : New. 2019. Paperback. . . . . .

Paperback. Etat : Brand New. 368 pages. 10.25x7.00x0.83 inches. In Stock.

Etat : New. In English.

Paperback. Etat : Brand New. 237 pages. 9.25x7.25x0.50 inches. In Stock.

Etat : New. 2019. Paperback. . . . . . Books ship from the US and Ireland.

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Taschenbuch. Etat : Neu. Computational Analysis of Structure Function and Evolution of Serpins | Protein Conformation and Enzymology Lab Department of Biosciences JMI | Poonam Singh (u. a.) | Taschenbuch | Englisch | LAP Lambert Academic Publishing | EAN 9783659246845 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu.…

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Hardcover. Etat : Brand New. 237 pages. 9.50x7.50x0.75 inches. In Stock.

Paperback. Etat : Brand New. 316 pages. 8.66x5.91x0.72 inches. In Stock.

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Etat : Hervorragend. Zustand: Hervorragend | Seiten: 256 | Sprache: Englisch | Produktart: Bücher | Provides a synthesis of our current understanding of hemoglobin (Hb) function and evolution, and illustrates how research on this protein has provided more general insights into mechanisms of protein evolution and biochemical adaptation.…

Hardcover. Etat : Brand New. 237 pages. 9.50x7.50x0.75 inches. In Stock.

Etat : gut. 1996. Ribosomal RNA : Structure, evolution, processing, and function in protein biosynthesis In deutscher Sprache. pages.

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Buch. Etat : Neu. Neuware - The primary aim of this book is to provide a synthesis of our current understanding of hemoglobin function and evolution, and to illustrate how research on one particular family of proteins has provided general insights into mechanisms of protein evolution and biochemical adaptation. In doing so, it will also promote an appreciation of how mechanistic insights into protein function can enrich our understanding of how evolution works. Reciprocally, it highlights how approaches in evolutionary genetics (such as phylogenetic comparative methods and ancestral sequence reconstruction) can be brought to bear on questions about the functional evolution of proteins. This treatise on the functional evolution of hemoglobin illustrates how research on a single, well-chosen model system can enhance our investigative acuity and bring key conceptual questions into especially sharp focus.…

Taschenbuch. Etat : Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Serine Protease inhibitors like antitrypsin, antichymotrypsin, C1-inhibitor, antithrombin and plasminogen activator inhibitor, play absolutely critical role in the control of proteinases, involved in the inflammatory, complement, coagulation and fibrinolytic pathways respectively, and are associated with diseases like emphysema/cirrhosis, angioedema, familial dementia, chronic obstructive bronchitis and thrombosis. The mechanism of inhibition of serpin requires large scale conformation change and native state of serpin is in a metastable state which transforms into a stable state when they inhibit target proteases. Serpins are prone to conformational diseases due to their susceptibility to undergo point mutations especially in mobile domains that can results in aberrant intermolecular linkage and polymer formation. The effects of such protein aggregation are cumulative, with a progressive loss of cellular function. Serpin polymerization is a significant problem and devising a cure has been cumbersome owing to their complex mechanism of inhibition, metastable nature, cofactor binding ability and large scale conformational change. Critical understanding of the factors and mechanisms.…

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