Peter Van Den Elsen (15 results)

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Taschenbuch. Condition: Neu. The Human T-Cell Receptor Repertoire and Transplantation | Peter Van Den Elsen | Taschenbuch | xi | Englisch | 2013 | Springer | EAN 9783662224960 | Verantwortliche Person für die EU: Springer Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg, juergen[dot]hartmann[at]springer[dot]com | Anbieter: preigu. …

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Taschenbuch. Condition: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -these analyses it became clear that the MHC class I molecule com prised a distinct groove on the external side of the molecule. The sides of the groove are formed by the a-helical structures of the a and a 1 2 domains and a floor which is formed by 8 anti-parallel 13 strands. The various polymorphic residues, as determined from DNA sequence analysis, are localized within these a-helices and 13-plated sheets within the groove. More importantly, these analyses also revealed the presence of elec tron-dense material in the groove. This material was subsequently iden 568 10 tified as a linear peptide of 8-10 amino acids long. - -- High resolu tion crystallographic analyses of the class I MHC structure have revealed the existence of so-called pockets within the grooves of the MHC class I molecules. These pockets designated A-F, exhibited allele-specificity and are directly involved in the binding of the peptide, primarily through interaction with the dominant anchor residues as found in MHC class I associated pep tides. 6,7,9,11 The class II MHC antigens consist on the cell surface of a 34 kD a chain non-covalently associated with a 28 kD 13 chain. With the excep tion of the DR a-chain, all other MHC class II a and 13 chains are poly morphic. 188 pp. Englisch.…

Taschenbuch. Condition: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - these analyses it became clear that the MHC class I molecule com prised a distinct groove on the external side of the molecule. The sides of the groove are formed by the a-helical structures of the a and a 1 2 domains and a floor which is formed by 8 anti-parallel 13 strands. The various polymorphic residues, as determined from DNA sequence analysis, are localized within these a-helices and 13-plated sheets within the groove. More importantly, these analyses also revealed the presence of elec tron-dense material in the groove. This material was subsequently iden 568 10 tified as a linear peptide of 8-10 amino acids long. - -- High resolu tion crystallographic analyses of the class I MHC structure have revealed the existence of so-called pockets within the grooves of the MHC class I molecules. These pockets designated A-F, exhibited allele-specificity and are directly involved in the binding of the peptide, primarily through interaction with the dominant anchor residues as found in MHC class I associated pep tides. 6,7,9,11 The class II MHC antigens consist on the cell surface of a 34 kD a chain non-covalently associated with a 28 kD 13 chain. With the excep tion of the DR a-chain, all other MHC class II a and 13 chains are poly morphic.…

Condition: New. Print on Demand pp. 188 66:B&W 7 x 10 in or 254 x 178 mm Perfect Bound on White w/Gloss Lam.

Condition: New. PRINT ON DEMAND pp. 188.

Taschenbuch. Condition: Neu. This item is printed on demand - Print on Demand Titel. Neuware -these analyses it became clear that the MHC class I molecule com prised a distinct groove on the external side of the molecule. The sides of the groove are formed by the a-helical structures of the a and a 1 2 domains and a floor which is formed by 8 anti-parallel 13 strands. The various polymorphic residues, as determined from DNA sequence analysis, are localized within these a-helices and 13-plated sheets within the groove. More importantly, these analyses also revealed the presence of elec tron-dense material in the groove. This material was subsequently iden 568 10 tified as a linear peptide of 8-10 amino acids long. ¿ ¿- High resolu tion crystallographic analyses of the class I MHC structure have revealed the existence of so-called pockets within the grooves of the MHC class I molecules. These pockets designated A-F, exhibited allele-specificity and are directly involved in the binding of the peptide, primarily through interaction with the dominant anchor residues as found in MHC class I associated pep tides. 6,7,9,11 The class II MHC antigens consist on the cell surface of a 34 kD a chain non-covalently associated with a 28 kD 13 chain. With the excep tion of the DR a-chain, all other MHC class II a and 13 chains are poly morphic.Springer-Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg 188 pp. Englisch.…