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Structural Characterization of a Microperoxidase Inside a Metal‐Directed Protein Cage
Author(s) -
Ni Thomas W.,
Tezcan F. Akif
Publication year - 2010
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.201001487
Subject(s) - crystallography , cage , crystal structure , histidine , metal , heme , chemistry , zinc , peptide , tetrahedron , protein crystallization , stereochemistry , nanotechnology , materials science , amino acid , organic chemistry , biochemistry , engineering , crystallization , enzyme , structural engineering
Caged to submission : The zinc‐ion‐directed assembly of tetrahedral protein cages (Zn 30 :CFMC‐1 12 ) in a rhombohedral crystal lattice is presented. The histidine side chains and exposed hydrophobic groups lining up the cavities of these cages enabled a flexible c ‐type heme peptide fragment (a microperoxidase) to be immobilized within and its crystal structure to be determined at 1.9 Å resolution.

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