| Autor: |
Walker, John M., Cabilly, Shmuel, Lu, Zhijan, Tripp, Brian C., McCoy, John M. |
| Zdroj: |
Combinatorial Peptide Library Protocols; 1998, p265-280, 16p |
| Abstrakt: |
A number of systems have been developed over recent years that allow the selection of sequences with desired binding specificities from highly diverse, randomly generated peptlde libraries (1-3), When a member of a peptide library mteracts with a target blomolecule during one of these selections, both its primary sequence and its conformation play Important roles in the recognition process However, typically in these systems the peptides are tethered to one end of a fusion partner protein, where they possess many degrees of conformatlonal freedom. These flexible peptides may possess lower affinities for their target mole cules than the same peptldes presented as part of a folded native protein structure or in a more constrained cyclic structure (4-7). To circumvent this problem, various "protein scaffolds" have been proposed to help small peptides retain their conformations by restricting chain flexibility (8-10). [ABSTRACT FROM AUTHOR] |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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