Document Type

Journal Article

Date of this Version

9-5-2007

Publication Source

Journal of the American Chemical Society

Volume

129

Issue

35

Start Page

10732

Last Page

10740

DOI

10.1021/ja071199j

Abstract

We describe the computational design of a single-chain four-helix bundle that noncovalently self-assembles with fully synthetic non-natural porphyrin cofactors. With this strategy, both the electronic structure of the cofactor as well as its protein environment may be varied to explore and modulate the functional and photophysical properties of the assembly. Solution characterization (NMR, UV-vis) of the protein showed that it bound with high specificity to the desired cofactors, suggesting that a uniquely structured protein and well-defined site had indeed been created. This provides a genetically expressed single-chain protein scaffold that will allow highly facile, flexible, and asymmetric variations to enable selective incorporation of different cofactors, surface-immobilization, and introduction of spectroscopic probes.

Copyright/Permission Statement

This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of the American Chemical Society, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see doi: 10.1021/ja071199j

Keywords

Amino Acid Sequence, Chromatography, Gel, Circular Dichroism, Metalloproteins, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Porphyrins, Protein Structure, Secondary, Spectrophotometry, Ultraviolet, Thermodynamics, Ultracentrifugation

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Date Posted: 07 December 2016

This document has been peer reviewed.