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Fibrous Nanostructures from the Self‐Assembly of Designed Repeat Protein Modules
Author(s) -
Phillips Jonathan J.,
Millership Charlotte,
Main Ewan R. G.
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201203795
Subject(s) - tetratricopeptide , monomer , block (permutation group theory) , computer science , protein engineering , nanotechnology , insert (composites) , aqueous solution , chemistry , computational biology , materials science , biochemistry , biology , gene , combinatorics , mathematics , organic chemistry , composite material , enzyme , polymer
Single‐protein‐chain superhelical filaments are obtained from monomeric repeat proteins by controlling the chemistry and solvent exposure at their terminal interfaces. The assembly was achieved in aqueous solution, at neutral pH value, and at room temperature. The building block was a recombinantly engineered designed tetratricopeptide repeat protein. Directed head‐to‐tail self‐assembly was driven by genetically encoded orthogonal native chemical ligation.