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Article

Metal-Assembled Modular Proteins: Toward Functional Protein Design

Martin A. Case*^† and George L. McLendon^‡

Department of Chemistry, The University of Vermont, Burlington, Vermont 05405, and Department of Chemistry, Princeton University, Princeton, New Jersey 08544

Acc. Chem. Res., 2004, 37 (10), pp 754–762

DOI: 10.1021/ar960245+

Publication Date (Web): August 12, 2004

To whom correspondence should be addressed. E-mail: martin.case@uvm.edu.

†

The University of Vermont.

‡

Princeton University.

George McLendon is Russell Wellman Moore Professor of Chemistry and Chair of the Department of Chemistry at Princeton University.

Martin Case is an assistant professor in the Department of Chemistry at the University of Vermont.

Abstract

Metal-assembled parallel helix-bundle proteins have been used to investigate electron transfer through α-helical structures. Fermi Golden Rule distance dependence of electron transfer rates was established in a family of designed metalloproteins, and the contribution of intrahelical hydrogen bonding to the matrix tunneling element was explored. The first steps toward the design of functional proteins using dynamic combinatorial assembly of α-helical structural elements are described.

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