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      In vitro selection and evolution of functional proteins by using ribosome display.

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          Abstract

          We report here a system with which a correctly folded complete protein and its encoding mRNA both remain attached to the ribosome and can be enriched for the ligand-binding properties of the native protein. We have selected a single-chain fragment (scFv) of an antibody 10(8)-fold by five cycles of transcription, translation, antigen-affinity selection, and PCR. The selected scFv fragments all mutated in vitro by acquiring up to four unrelated amino acid exchanges over the five generations, but they remained fully compatible with antigen binding. Libraries of native folded proteins can now be screened and made to evolve in a cell-free system without any transformation or constraints imposed by the host cell.

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          Author and article information

          Journal
          Proc Natl Acad Sci U S A
          Proceedings of the National Academy of Sciences of the United States of America
          Proceedings of the National Academy of Sciences
          0027-8424
          0027-8424
          May 13 1997
          : 94
          : 10
          Affiliations
          [1 ] Biochemisches Institut, Universität Zürich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.
          Article
          10.1073/pnas.94.10.4937
          24609
          9144168
          2a06c009-1869-4f47-b25e-71736852370e
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