Display ribosomal

Bacterial cell surface display Yeast cell surface display Mammalian cell surface display Ribosomal display Plasmid display... 

Ribosomal Protein Synthesis Inhibitors. Figure 5 Nucleotides at the binding sites of chloramphenicol, erythromycin and clindamycin at the peptidyl transferase center. The nucleotides that are within 4.4 A of the antibiotics chloramphenicol, erythromycin and clindamycin in 50S-antibiotic complexes are indicated with the letters C, E, and L, respectively, on the secondary structure of the peptidyl transferase loop region of 23S rRNA (the sequence shown is that of E. coll). The sites of drug resistance in one or more peptidyl transferase antibiotics due to base changes (solid circles) and lack of modification (solid square) are indicated. Nucleotides that display altered chemical reactivity in the presence of one or more peptidyl transferase antibiotics are boxed. 

Hanes, J. and Pluckthun, A. (1997) In vitro selection and evolution of functional proteins by using ribosome display. Proceedings of the National Academy of Sciences of the United States of America, 94, 4937-4942. 

He, M. and Khan, F. 2005. Ribosome display next generation display technologies for production of antibodies in vitro. Expert Review of Proteomics 2(3), 421-430. 

Calorimetric studies have been made on proteins S4, S7, S8, S15, S16, S18, Lll, and L7 (Khechinashvili et al., 1978 Gudkov and Behike, 1978). Most of these proteins displayed a cooperative tertiary structure in solution. Proteins S4, S7, SI5, and SI8 were extracted from the ribosome by a urea-LiCl technique followed by renaturation, whereas proteins S8, S16, and Lll were prepared by the mild isolation method. A calorimetric study on protein SI showed a noncooperative transition around 70-80 C, suggesting a flexible tertiary structure (L. Giri, unpublished). 

The results of a deconfounding experiment that distinguishe between the AB and the CD interaction were displayed in Figure 2. These data indicate that the interaction between the percent dissolved oxygen and buffers (CD) was important for the vesicle to ribosome ratio (Figure 2b) and not for the yield (Figure 2a). Since the CD interaction is not important to the yield the interaction between yeast extract and amino acid types (tiie AB interaction in the first experiment) must have been important for the yield. In this way, the affect of each interaction on the responses can be determined. 

---