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Literature DB >> 22234390

Electrochemical and structural coupling of the naphthoquinone amino acid.

Bruce R Lichtenstein¹, Veronica R Moorman, José F Cerda, A Joshua Wand, P Leslie Dutton.

Abstract

As a prelude to engineering artificial energy conversion proteins emulating biology, we examine the inclusion of a synthetic naphthoquinone amino acid in a characterized host-guest protein and determine the effects of its quinone and hydroquinone forms on the helix-coil distribution. This journal is © The Royal Society of Chemistry 2012

Entities: Chemical Gene

Mesh：

Substances：

Year: 2012 PMID： 22234390 PMCID： PMC3547611 DOI： 10.1039/c2cc16968a

Source DB: PubMed Journal: Chem Commun (Camb) ISSN： 1359-7345 Impact factor: 6.222

17 in total

Review 1. Flavoenzymes: diverse catalysts with recurrent features.

Authors: M W Fraaije; A Mattevi
Journal: Trends Biochem Sci Date: 2000-03 Impact factor: 13.807

2. The enthalpy of the alanine peptide helix measured by isothermal titration calorimetry using metal-binding to induce helix formation.

Authors: Maria M Lopez; Der-Hang Chin; Robert L Baldwin; George I Makhatadze
Journal: Proc Natl Acad Sci U S A Date: 2002-01-29 Impact factor: 11.205

3. The geometry and efficacy of cation-pi interactions in a diagonal position of a designed beta-hairpin.

Authors: Chad D Tatko; Marcey L Waters
Journal: Protein Sci Date: 2003-11 Impact factor: 6.725

4. Experimental investigation of initial steps of helix propagation in model peptides.

Authors: Grazyna Goch; Maciej Maciejczyk; Marta Oleszczuk; Damian Stachowiak; Joanna Malicka; Andrzej Bierzyński
Journal: Biochemistry Date: 2003-06-10 Impact factor: 3.162

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Authors: Charles J Reedy; Brian R Gibney
Journal: Chem Rev Date: 2004-02 Impact factor: 60.622

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Authors: S Ghisla; V Massey
Journal: Eur J Biochem Date: 1989-04-15

7. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy.

Authors: D S Wishart; B D Sykes; F M Richards
Journal: Biochemistry Date: 1992-02-18 Impact factor: 3.162

Electrochemical and structural coupling of the naphthoquinone amino acid.

Review 1. Flavoenzymes: diverse catalysts with recurrent features.

2. The enthalpy of the alanine peptide helix measured by isothermal titration calorimetry using metal-binding to induce helix formation.

3. The geometry and efficacy of cation-pi interactions in a diagonal position of a designed beta-hairpin.

4. Experimental investigation of initial steps of helix propagation in model peptides.

Review 5. Heme protein assemblies.

Review 6. Mechanisms of flavoprotein-catalyzed reactions.

7. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy.

8. Unusually stable helix formation in short alanine-based peptides.

9. Elucidating the folding problem of helical peptides using empirical parameters.

10. Reversible proton coupled electron transfer in a peptide-incorporated naphthoquinone amino acid.

1. Design and engineering of a man-made diffusive electron-transport protein.

2. First principles design of a core bioenergetic transmembrane electron-transfer protein.

3. Designing Light-Activated Charge-Separating Proteins with a Naphthoquinone Amino Acid.