This book provides, through X-ray crystallography, information about the structure and function relationships of urease and cytochrome c-553 from Bacillus pasteurii. Urease is a nickel enzyme involved in nitrogen turnover and in human and animal pathologies. The comparison between the native and the inhibited structures provides information about the active site and the inhibition mechanisms, and allows the proposal of a reaction mechanism which agrees with the available biochemical data. Cytochrome c-553 is a small electron transfer protein. The characterisation at atomic resolution (0.97 A) provides one of the most accurate heme structures to date. Providing a thoroughly written background and an accurate description of all the steps from bacterial growth to structure solution, this book is aimed at researchers interested in structural biology, in protein science and enzymatic catalysis. Useful for graduate and PhD students who are interested in protein crystallography. An easy to read background of protein crystallography is provided in the appendix for the less experienced reader.
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Stefano Benini, PhD: Master in Agricultural Science at the University of Bologna, PhD in Chemistry at the University of York and EMBL Hamburg, Postdoctoral fellow at the ICGEB Trieste and YSBL York, Protein crystallographer at the AstraZeneca Alderley Park, Professor in the Faculty of Science and Technology of the Free University of Bolzano
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Taschenbuch. Zustand: Neu. Structure and function of urease and cytochrome c-553 | A scientific journey to unravel the mechanism of urea enzymatic hydrolysis, and the role of cytochrome c-553 | Stefano Benini | Taschenbuch | 200 S. | Englisch | 2010 | LAP LAMBERT Academic Publishing | EAN 9783838364988 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu. Artikel-Nr. 101097438
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