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Your search keyword '"Thai, Corrine K."' showing total 9 results
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9 results on '"Thai, Corrine K."'

1. Nonequilibrium synthesis and assembly of hybrid inorganic-protein nanostructures using an engineered DNA binding protein

Author

Haixia Dai, Woo-Seok Choe, Thai, Corrine K., Sarikaya, Mehmet, Traxler, Beth A., Baneyx, Francois, and Schwartz, Daniel T.

Subjects
DNA binding proteins -- Structure, DNA binding proteins -- Chemical properties, Mass spectrometry -- Analysis, Oxidation-reduction reaction -- Analysis, Chemistry
Abstract

The nonequilibrium synthesis of Cu2O nanoparticles is accomplished using an engineered derivative of the DNA-binding protein Tral in a room-temperature precursor electrolyte. The results show that a protein with no intrinsic inorganic synthesis activity can be endowed with the ability to control the formation of inorganic nanostructures under thermodynamically unfavorable conditions, reproducing a key feature of biological hard-tissue growth and assembly.

Published
2005

8. Identification and characterization of Cu(2)O- and ZnO-binding polypeptides by Escherichia coli cell surface display: toward an understanding of metal oxide binding.

Author

Thai CK, Dai H, Sastry MS, Sarikaya M, Schwartz DT, and Baneyx F

Subjects
Amino Acid Motifs genetics, Amino Acid Sequence, Arginine chemistry, Arginine genetics, Arginine metabolism, Bacterial Adhesion genetics, Computer Simulation, Copper chemistry, Flagellin genetics, Glycine chemistry, Glycine genetics, Glycine metabolism, Hydrophobic and Hydrophilic Interactions, Isoelectric Point, Membrane Proteins chemistry, Membrane Proteins genetics, Membrane Proteins metabolism, Microscopy, Fluorescence, Models, Molecular, Peptide Library, Peptides chemistry, Peptides genetics, Protein Binding genetics, Recombinant Fusion Proteins chemistry, Recombinant Fusion Proteins genetics, Recombinant Fusion Proteins metabolism, Sequence Analysis, Protein, Static Electricity, Thioredoxins genetics, Tryptophan chemistry, Tryptophan genetics, Tryptophan metabolism, Zinc Oxide chemistry, Copper metabolism, Escherichia coli genetics, Peptides metabolism, Zinc Oxide metabolism
Abstract

We have used the FliTrx cell surface display system to identify disulfide-constrained dodecapeptides binding to the semiconducting metal oxides Cu(2)O and ZnO. Sequence analysis of the inserts revealed that the two populations exhibit similar, yet subtly different patterns of amino acid usage. Both sets of binders were enriched in arginine, tryptophan, and glycine with a higher degree of positional preference in the case of Cu(2)O binders. Tyrosine, proline, and serine were underrepresented in both populations. Peptides binding electrodeposited Cu(2)O or ZnO with high avidity could be subdivided into two classes based on pI and hydrophilicity. In the hydrophilic and positively charged Class I binders, the Arg-X-X-Arg tetrapeptide appears to be implicated in metal oxide binding, whereas Arg-Arg and Arg-Lys pairs allow for discrimination between Cu(2)O and ZnO. Molecular dynamics simulations of the disulfide-constrained peptides suggest that the aforementioned motifs are important to properly orient two basic residues that are likely to contact the metal oxides. The implications of our results in understanding the rules governing the interaction between peptides and inorganic compounds and in their use for the design of hybrid nanoarchitectures are discussed., (Copyright 2004 Wiley Periodicals, Inc.)

Published
2004
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