G proteins are molecular amplifiers. GTPases are a large family of enzymes that can bind and hydrolyze GTP. The GTP binding and hydrolysis takes place in the highly conserved G domain common to all GTPases. Protein crystal contacts are weak and generally form only under conditions designed to limit protein solubility and maximize protein-2 interactions. However, they do form with a kind of specificity, at least in the sense that only certain contacts are repeated within each unit cell of any particular crystal packing arrangement. For oligomeric proteins, amino acids at the subunit interfaces have been selected in order to maintain affinity and specificity properties. Many proteins contain highly flexible or even completely unfolded fragments that dramatically interfere with crystallization conditions. These conditions are the crystal lattice and Oligomeric interface or proteins that allow the residues to bind in such a specific way by which the crystallization of GTPase is fast. This book therefore, should be helpful for better understanding the crystallograpgy of proteins for biologists etc.
Les informations fournies dans la section « Synopsis » peuvent faire référence à une autre édition de ce titre.
Vendeur : BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Allemagne
Taschenbuch. Etat : Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -G proteins are molecular amplifiers. GTPases are a large family of enzymes that can bind and hydrolyze GTP. The GTP binding and hydrolysis takes place in the highly conserved G domain common to all GTPases. Protein crystal contacts are weak and generally form only under conditions designed to limit protein solubility and maximize protein-2 interactions. However, they do form with a kind of specificity, at least in the sense that only certain contacts are repeated within each unit cell of any particular crystal packing arrangement. For oligomeric proteins, amino acids at the subunit interfaces have been selected in order to maintain affinity and specificity properties. Many proteins contain highly flexible or even completely unfolded fragments that dramatically interfere with crystallization conditions. These conditions are the crystal lattice and Oligomeric interface or proteins that allow the residues to bind in such a specific way by which the crystallization of GTPase is fast. This book therefore, should be helpful for better understanding the crystallograpgy of proteins for biologists etc. 52 pp. Englisch. N° de réf. du vendeur 9783659914973
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Vendeur : Revaluation Books, Exeter, Royaume-Uni
Paperback. Etat : Brand New. 52 pages. 8.66x5.91x0.12 inches. In Stock. N° de réf. du vendeur 3659914975
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Etat : New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Jaiswal Ashish KumarMr. Jaiswal earned his MS in Bioinformatics from CCS University India 2005. He has many publications during his 13 years of research experience at various institutes (ICAR, ICMR, NYUAD). He published a course book. N° de réf. du vendeur 159147547
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Vendeur : buchversandmimpf2000, Emtmannsberg, BAYE, Allemagne
Taschenbuch. Etat : Neu. This item is printed on demand - Print on Demand Titel. Neuware -G proteins are molecular amplifiers. GTPases are a large family of enzymes that can bind and hydrolyze GTP. The GTP binding and hydrolysis takes place in the highly conserved G domain common to all GTPases. Protein crystal contacts are weak and generally form only under conditions designed to limit protein solubility and maximize protein-2 interactions. However, they do form with a kind of specificity, at least in the sense that only certain contacts are repeated within each unit cell of any particular crystal packing arrangement. For oligomeric proteins, amino acids at the subunit interfaces have been selected in order to maintain affinity and specificity properties. Many proteins contain highly flexible or even completely unfolded fragments that dramatically interfere with crystallization conditions. These conditions are the crystal lattice and Oligomeric interface or proteins that allow the residues to bind in such a specific way by which the crystallization of GTPase is fast. This book therefore, should be helpful for better understanding the crystallograpgy of proteins for biologists etc.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 52 pp. Englisch. N° de réf. du vendeur 9783659914973
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Vendeur : AHA-BUCH GmbH, Einbeck, Allemagne
Taschenbuch. Etat : Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - G proteins are molecular amplifiers. GTPases are a large family of enzymes that can bind and hydrolyze GTP. The GTP binding and hydrolysis takes place in the highly conserved G domain common to all GTPases. Protein crystal contacts are weak and generally form only under conditions designed to limit protein solubility and maximize protein-2 interactions. However, they do form with a kind of specificity, at least in the sense that only certain contacts are repeated within each unit cell of any particular crystal packing arrangement. For oligomeric proteins, amino acids at the subunit interfaces have been selected in order to maintain affinity and specificity properties. Many proteins contain highly flexible or even completely unfolded fragments that dramatically interfere with crystallization conditions. These conditions are the crystal lattice and Oligomeric interface or proteins that allow the residues to bind in such a specific way by which the crystallization of GTPase is fast. This book therefore, should be helpful for better understanding the crystallograpgy of proteins for biologists etc. N° de réf. du vendeur 9783659914973
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Vendeur : preigu, Osnabrück, Allemagne
Taschenbuch. Etat : Neu. Comparative Analysis of Contacts Between Crystal Lattice & Oligo Interface | Ashish Kumar Jaiswal | Taschenbuch | 52 S. | Englisch | 2016 | LAP LAMBERT Academic Publishing | EAN 9783659914973 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu. N° de réf. du vendeur 103491244
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