Combinatorial peptide library protocols (32 résultats)

Etat : very_good. Gently read. May have name of previous ownership, or ex-library edition. Binding tight; spine straight and smooth, with no creasing; covers clean and crisp. Minimal signs of handling or shelving. 100% GUARANTEE! Shipped with delivery confirmation, if you're not satisfied with purchase please return item! Ships USPS Media Mail.…

hardcover. Etat : Good. Ex- library copy with stamps and stickers.

Etat : Brand New. New. US edition. Expediting shipping for all USA and Europe orders excluding PO Box. Excellent Customer Service.

Etat : New.

Etat : New.

Etat : New.

Hardcover. Etat : New. In shrink wrap. Looks like an interesting title.

Etat : As New. Unread book in perfect condition.

Etat : As New. Unread book in perfect condition.

Etat : 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. . . . .

Etat : New. In English.

Etat : 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. . . . . …

Etat : New. pp. 328.

Taschenbuch. Etat : 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. …

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

Etat : 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. …

Etat : New. In English.

Etat : New. pp. 332.

Etat : New. pp. 332.

Etat : New. Satisfaction Guaranteed or your money back.

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

Taschenbuch. Etat : 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. Etat : 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.…

Etat : 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.…

Etat : 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. Etat : 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. Etat : 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. Etat : 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. …

Buch. Etat : Neu. This item is printed on demand - Print on Demand Titel. 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.Springer-Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg 332 pp. Englisch.…