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Dôr hédde de skut. De geschiedenis van de Gemertse gilden
Published by Heemkundekring De Kammonderij Gemert, Gemert, 1982
Condition: Good.
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Condition: As New. Unread book in perfect condition.
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The Human T-Cell Receptor Repertoire and Transplantation (Molecular Biology Intelligence Unit)
Seller: Ria Christie Collections, Uxbridge, United Kingdom
Seller rating 5 out of 5 stars
£ 96.88
£ 11.98 shipping
Ships from United Kingdom to U.S.A.Quantity: Over 20 available
Add to basketCondition: New. In.
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Condition: New.
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Human T-cell Receptor Repertoire and Transplantation
Seller: GreatBookPricesUK, Woodford Green, United Kingdom
Seller rating 5 out of 5 stars
Condition: New.
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Human T-cell Receptor Repertoire and Transplantation
Seller: GreatBookPricesUK, Woodford Green, United Kingdom
Seller rating 5 out of 5 stars
£ 107.98
£ 15 shipping
Ships from United Kingdom to U.S.A.Quantity: Over 20 available
Add to basketCondition: As New. Unread book in perfect condition.
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The Human T-Cell Receptor Repertoire and Transplantation
Language: English
Published by Springer Berlin Heidelberg, 2013
ISBN 10: 3662224968 ISBN 13: 9783662224960
Condition: New.
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Condition: New. pp. 188.
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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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The Human T-Cell Receptor Repertoire and Transplantation
Language: English
Published by Springer Berlin Heidelberg, 2013
ISBN 10: 3662224968 ISBN 13: 9783662224960
Taschenbuch. Condition: Neu. Druck auf Anfrage 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.
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Condition: new. Questo è un articolo print on demand.
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The Human T-Cell Receptor Repertoire and Transplantation
Language: English
Published by Springer Berlin Heidelberg, Springer Berlin Heidelberg Nov 2013, 2013
ISBN 10: 3662224968 ISBN 13: 9783662224960
Seller: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Germany
Seller rating 5 out of 5 stars
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.
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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.
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Condition: New. PRINT ON DEMAND pp. 188.
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The Human T-Cell Receptor Repertoire and Transplantation
Language: English
Published by Springer Berlin Heidelberg, Springer Nov 2013, 2013
ISBN 10: 3662224968 ISBN 13: 9783662224960
Seller: buchversandmimpf2000, Emtmannsberg, BAYE, Germany
Seller rating 5 out of 5 stars
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.
