Combinatorial peptide library protocols (33 Ergebnisse)

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hardcover. Zustand: Very Good. Combinatorial Peptide Library Protocols: 87 (Methods in Molecular Biology, 87) This book is in very good condition and will be shipped within 24 hours of ordering. The cover may have some limited signs of wear but the pages are clean, intact and the spine remains undamaged. This book has clearly been well maintained and looked after thus far. Money back guarantee if you are not satisfied. See all our books here, order more than 1 book and get discounted shipping. .…

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Zustand: New. Editor(s): Cabilly, Shmuel. Series: Methods in Molecular Biology. Num Pages: 313 pages, biography. BIC Classification: PSB. Category: (P) Professional & Vocational. Dimension: 229 x 152 x 18. Weight in Grams: 484. . 2010. 1st ed. Softcover of orig. ed. 1998. Paperback. . . . .

Zustand: New. A collection of techniques for the construction and use of peptide libraries. It contains methods that include protocols for the chemical synthesis of peptide libraries, and for constructing peptide libraries that are displayed on the surface of filamentous phage or bacteria. Editor(s): Cabilly, S. Series: Methods in Molecular Biology. Num Pages: 313 pages, biography. BIC Classification: PNN; PSBC; PSD. Category: (P) Professional & Vocational; (UP) Postgraduate, Research & Scholarly; (UU) Undergraduate. Dimension: 235 x 155 x 26. Weight in Grams: 721. . 1997. Hardback. . . . . …

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Taschenbuch. Zustand: Neu. Combinatorial Peptide Library Protocols | Shmuel Cabilly | Taschenbuch | xiii | Englisch | 2010 | Humana Press | EAN 9781617370229 | Verantwortliche Person für die EU: Humana Press in Springer Science + Business Media, Heidelberger Platz 3, 14197 Berlin, juergen[dot]hartmann[at]springer[dot]com | Anbieter: preigu. …

Zustand: New. Editor(s): Cabilly, Shmuel. Series: Methods in Molecular Biology. Num Pages: 313 pages, biography. BIC Classification: PSB. Category: (P) Professional & Vocational. Dimension: 229 x 152 x 18. Weight in Grams: 484. . 2010. 1st ed. Softcover of orig. ed. 1998. Paperback. . . . . Books ship from the US and Ireland.…

Hardcover. Zustand: Brand New. 313 pages. 9.50x6.50x1.00 inches. In Stock.

Zustand: New. A collection of techniques for the construction and use of peptide libraries. It contains methods that include protocols for the chemical synthesis of peptide libraries, and for constructing peptide libraries that are displayed on the surface of filamentous phage or bacteria. Editor(s): Cabilly, S. Series: Methods in Molecular Biology. Num Pages: 313 pages, biography. BIC Classification: PNN; PSBC; PSD. Category: (P) Professional & Vocational; (UP) Postgraduate, Research & Scholarly; (UU) Undergraduate. Dimension: 235 x 155 x 26. Weight in Grams: 721. . 1997. Hardback. . . . . Books ship from the US and Ireland. …

Zustand: New. In English.

Zustand: New. pp. 332.

Zustand: New. pp. 332.

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Zustand: new. Questo è un articolo print on demand.

Taschenbuch. Zustand: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -During the course of evolution, an imbalance was created between the rate of vertebrate genetic adaptation and that of the lower forms of living organisms, such as bacteria and viruses. This imbalance has given the latter the advantage of generating, relatively quickly, molecules with unexpected structures and features that carry a threat to vertebrates. To compensate for their weakness, vertebrates have accelerated their own evolutionary processes, not at the level of whole organism, but in specialized cells containing the genes that code for antibody molecules or for T-cell receptors. That is, when an immediate requirement for molecules capable of specific interactions arose, nature has preferred to speed up the mode of Darwinian evolution in pref- ence to any other approach (such as the use of X-ray diffraction studies and computergraphic analysis). Recently, Darwinian rules have been adapted for test tube research, and the concept of selecting molecules having particular characteristics from r- dom pools has been realized in the form of various chemical and biological combinatorial libraries. While working with these libraries, we noticed the interesting fact that when combinatorial libraries of oligopeptides were allowed to interact with different selector proteins, only the actual binding sites of these proteins showed binding properties, whereas the rest of the p- tein surface seemed 'inert. ' This seemingly common feature of protein- having no extra potential binding sites--was probably selected during evolution in order to minimize nonspecific interactions with the surrounding milieu. 313 pp. Englisch.…

Buch. Zustand: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -During the course of evolution, an imbalance was created between the rate of vertebrate genetic adaptation and that of the lower forms of living organisms, such as bacteria and viruses. This imbalance has given the latter the advantage of generating, relatively quickly, molecules with unexpected structures and features that carry a threat to vertebrates. To compensate for their weakness, vertebrates have accelerated their own evolutionary processes, not at the level of whole organism, but in specialized cells containing the genes that code for antibody molecules or for T-cell receptors. That is, when an immediate requirement for molecules capable of specific interactions arose, nature has preferred to speed up the mode of Darwinian evolution in pref- ence to any other approach (such as the use of X-ray diffraction studies and computergraphic analysis). Recently, Darwinian rules have been adapted for test tube research, and the concept of selecting molecules having particular characteristics from r- dom pools has been realized in the form of various chemical and biological combinatorial libraries. While working with these libraries, we noticed the interesting fact that when combinatorial libraries of oligopeptides were allowed to interact with different selector proteins, only the actual binding sites of these proteins showed binding properties, whereas the rest of the p- tein surface seemed 'inert. ' This seemingly common feature of protein- having no extra potential binding sites--was probably selected during evolution in order to minimize nonspecific interactions with the surrounding milieu. 332 pp. Englisch.…

Zustand: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. During the course of evolution, an imbalance was created between the rate of vertebrate genetic adaptation and that of the lower forms of living organisms, such as bacteria and viruses. This imbalance has given the latter the advantage of generating, relati. …

Zustand: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. During the course of evolution, an imbalance was created between the rate of vertebrate genetic adaptation and that of the lower forms of living organisms, such as bacteria and viruses. This imbalance has given the latter the advantage of generating, relati. …

Taschenbuch. Zustand: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - During the course of evolution, an imbalance was created between the rate of vertebrate genetic adaptation and that of the lower forms of living organisms, such as bacteria and viruses. This imbalance has given the latter the advantage of generating, relatively quickly, molecules with unexpected structures and features that carry a threat to vertebrates. To compensate for their weakness, vertebrates have accelerated their own evolutionary processes, not at the level of whole organism, but in specialized cells containing the genes that code for antibody molecules or for T-cell receptors. That is, when an immediate requirement for molecules capable of specific interactions arose, nature has preferred to speed up the mode of Darwinian evolution in pref- ence to any other approach (such as the use of X-ray diffraction studies and computergraphic analysis). Recently, Darwinian rules have been adapted for test tube research, and the concept of selecting molecules having particular characteristics from r- dom pools has been realized in the form of various chemical and biological combinatorial libraries. While working with these libraries, we noticed the interesting fact that when combinatorial libraries of oligopeptides were allowed to interact with different selector proteins, only the actual binding sites of these proteins showed binding properties, whereas the rest of the p- tein surface seemed 'inert. ' This seemingly common feature of protein- having no extra potential binding sites--was probably selected during evolution in order to minimize nonspecific interactions with the surrounding milieu.…

Buch. Zustand: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - During the course of evolution, an imbalance was created between the rate of vertebrate genetic adaptation and that of the lower forms of living organisms, such as bacteria and viruses. This imbalance has given the latter the advantage of generating, relatively quickly, molecules with unexpected structures and features that carry a threat to vertebrates. To compensate for their weakness, vertebrates have accelerated their own evolutionary processes, not at the level of whole organism, but in specialized cells containing the genes that code for antibody molecules or for T-cell receptors. That is, when an immediate requirement for molecules capable of specific interactions arose, nature has preferred to speed up the mode of Darwinian evolution in pref- ence to any other approach (such as the use of X-ray diffraction studies and computergraphic analysis). Recently, Darwinian rules have been adapted for test tube research, and the concept of selecting molecules having particular characteristics from r- dom pools has been realized in the form of various chemical and biological combinatorial libraries. While working with these libraries, we noticed the interesting fact that when combinatorial libraries of oligopeptides were allowed to interact with different selector proteins, only the actual binding sites of these proteins showed binding properties, whereas the rest of the p- tein surface seemed 'inert. ' This seemingly common feature of protein- having no extra potential binding sites--was probably selected during evolution in order to minimize nonspecific interactions with the surrounding milieu.…

Buch. Zustand: Neu. Combinatorial Peptide Library Protocols | Shmuel Cabilly | Buch | Einband - fest (Hardcover) | Englisch | 1997 | Humana | EAN 9780896033924 | Verantwortliche Person für die EU: Springer Nature Customer Service Center GmbH, Europaplatz 3, 69115 Heidelberg, productsafety[at]springernature[dot]com | Anbieter: preigu Print on Demand. …