Combinatorial Peptide Library ProtocolsShmuel Cabilly Springer Science & Business Media, 2 feb. 2008 - 313 pagini 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. |
Cuprins
Synthesis and Screening of Positional Scanning Combinatorial | 13 |
Displaying Libraries on Conformationally Constrained Peptides | 25 |
Libraries from Libraries Chemical Transformation | 41 |
Preparation of Biocompatible Resins for Library Syntheses | 59 |
The SolidPhase Enzyme Inhibitor Library Assay | 75 |
Analysis of Protein Kinase Substrate Specificity by the | 99 |
Generation of Multiuse Peptide Libraries for Functional Screenings | 107 |
Functional Screening of Multiuse Peptide Libraries Using | 119 |
Conformational Mimicry Through Random Constraints Plus Affinity | 165 |
The Use of Combinatorial Libraries to Identify Ligands That Interact | 175 |
Screening Phage Display Peptide Libraries on Nitrocellulose | 185 |
Identification of DiseaseSpecific Epitopes | 195 |
Identification of Peptide Ligands for the Antigen Binding Receptor | 209 |
Major Histocompatibility Complex AlleleSpecific Peptide Libraries | 235 |
Phage Display of Peptide Libraries on Protein Scaffolds | 249 |
Combinatorial Peptide Library as an Immunogen | 281 |
The Basic Structure of Filamentous Phage and Its | 129 |
Construction and Use of a 20mer Phage Display Epitope Library | 137 |
Construction of DisulfideConstrained Random Peptide Libraries | 155 |
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Termeni și expresii frecvente
affinity agar aliquots amino acids ampicillin antibody antigen assay autoclave bacteria beads binding biotinylated Cabilly Centrifuge cleavage clones coat coli column combinatorial libraries Combinatorial Peptide Library concentration containing coupling Deprotect described in Subheading dichloromethane dilution Dissolve electroporation ELISA plates eluted enzyme epitope ethanol filamentous phage filters gene h at room Houghten Incubate inhibitors IPTG ligands ligation medium melanophores Meldal membrane method mg/mL mixotope mixture mmol Molecular motifs MUPL NaCl Natl nitrocellulose Note oligonucleotide overnight peptide libraries Peptide Library Protocols peptide ligands peptide synthesis phage display phage library phagemid phosphorylation pIII piperidine pipet prepared protein kinases purified pVIII random reaction reagents receptor remove room temperature screening selection sequence shaking sIgR specific step sterile stock solution substrate supernatant synthetic peptide tetracycline titer transfer Tris-HCl tube tumor cells vector Wash the resin XL1-blue µg/mL
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Artificial DNA: Methods and Applications Yury E. Khudyakov,Howard A. Fields Nu există previzualizare disponibilă - 2002 |