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Biochemistry, Biophysics, and Structural Biology Commons

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Series

Proteins

University of Pennsylvania

Publication Year

Articles 1 - 3 of 3

Full-Text Articles in Biochemistry, Biophysics, and Structural Biology

Computational De Novo Design And Characterization Of A Protein That Selectively Binds A Highly Hyperpolarizable Abiological Chromophore, H Christopher Fry, Andreas Lehmann, Louise E. Sinks, Inge Asselberghs, Andrey Tronin, Venkata Krishnan, J Kent Blasie, Koen Clays, William F. Degrado, Jeffery G. Saven, Michael J. Therien Sep 2013

Computational De Novo Design And Characterization Of A Protein That Selectively Binds A Highly Hyperpolarizable Abiological Chromophore, H Christopher Fry, Andreas Lehmann, Louise E. Sinks, Inge Asselberghs, Andrey Tronin, Venkata Krishnan, J Kent Blasie, Koen Clays, William F. Degrado, Jeffery G. Saven, Michael J. Therien

Departmental Papers (Chemistry)

This work reports the first example of a single-chain protein computationally designed to contain four α-helical segments and fold to form a four-helix bundle encapsulating a supramolecular abiological chromophore that possesses exceptional nonlinear optical properties. The 109-residue protein, designated SCRPZ-1, binds and disperses an insoluble hyperpolarizable chromophore, ruthenium(II) [5-(4'-ethynyl-(2,2';6',2″-terpyridinyl))-10,20-bis(phenyl)porphinato]zinc(II)-(2,2';6',2″-terpyridine)(2+) (RuPZn) in aqueous buffer solution at a 1:1 stoichiometry. A 1:1 binding stoichiometry of the holoprotein is supported by electronic absorption and circular dichroism spectra, as well as equilibrium ...


Computational Protein Design: Engineering Molecular Diversity, Nonnatural Enzymes, Nonbiological Cofactor Complexes, And Membrane Proteins, Jeffery G. Saven Jun 2011

Computational Protein Design: Engineering Molecular Diversity, Nonnatural Enzymes, Nonbiological Cofactor Complexes, And Membrane Proteins, Jeffery G. Saven

Departmental Papers (Chemistry)

Computational and theoretical methods are advancing protein design as a means to create and investigate proteins. Such efforts further our capacity to control, design and understand biomolecular structure, sequence and function. Herein, the focus is on some recent applications that involve using theoretical and computational methods to guide the design of protein sequence ensembles, new enzymes, proteins with novel cofactors, and membrane proteins.


Computational Design And Elaboration Of A De Novo Heterotetrameric Α-Helical Protein That Selectively Binds An Emissive Abiological (Porphinato)Zinc Chromophore, H Christopher Fry, Andreas Lehmann, Jeffery G. Saven, William F. Degrado, Michael J. Therien Mar 2010

Computational Design And Elaboration Of A De Novo Heterotetrameric Α-Helical Protein That Selectively Binds An Emissive Abiological (Porphinato)Zinc Chromophore, H Christopher Fry, Andreas Lehmann, Jeffery G. Saven, William F. Degrado, Michael J. Therien

Departmental Papers (Chemistry)

The first example of a computationally de novo designed protein that binds an emissive abiological chromophore is presented, in which a sophisticated level of cofactor discrimination is pre-engineered. This heterotetrameric, C(2)-symmetric bundle, A(His):B(Thr), uniquely binds (5,15-di[(4-carboxymethyleneoxy)phenyl]porphinato)zinc [(DPP)Zn] via histidine coordination and complementary noncovalent interactions. The A(2)B(2) heterotetrameric protein reflects ligand-directed elements of both positive and negative design, including hydrogen bonds to second-shell ligands. Experimental support for the appropriate formulation of [(DPP)Zn:A(His):B(Thr)](2) is provided by UV/visible and circular dichroism spectroscopies ...