De novo design of metalloproteins with variant hydrophobic core | Posted on:2010-03-30 | Degree:Ph.D | Type:Dissertation | University:Bowling Green State University | Candidate:Xie, Fei | Full Text:PDF | GTID:1441390002980346 | Subject:Physical chemistry | Abstract/Summary: | | This work studies a series of related de novo designed luminescent Cu(I) metalloproteins having different cysteine-based metal binding sites within the hydrophobic cores. The peptide sequences are based on the (I a-Eb-Ac-L d-Ee-Gf-K g)n heptad repeat which is known to form two-stranded coiled coil in aqueous solution. The metal-binding cysteine residues are placed at the hydrophobic a and/or d positions in the middle of the peptide sequences. With subtle changes of the metal-binding site, the resultant Cu(I) metalloproteins give distinctly different structures and properties.;The peptide C16C19GGY exists as a random coil and the Cu(I)-C16C19GGY metalloprotein exists as a 4-helix bundle (Cu4P4, P = peptide) which gives strong room temperature emission at 600 nm. The peptide C12C16GGY exists as a random coil and the Cu(I)-C12C16GGY metalloprotein exists as a 4-helix bundle (Cu4P4) which gives strong room temperature emission at 575 nm. The peptide C12C16C19GGY exists as a random coil and the Cu(I)-C12C16C19GGY metalloprotein exists as a 4-helix bundle (Cu8P4) which gives strong room temperature emission at 605 nm. The peptide C12C19GGY exists as a random coil and the Cu(I)-C12C19GGY metalloprotein also exists as a random coil (Cu4P4) which gives strong room temperature emission at 600 nm. The peptide C16GGY, C19GGY exist as two-stranded coiled-coils and the Cu(I)-C16GGY, Cu(I)-C19GGY metalloproteins exist as 4-helix bundles (Cu3P4) which gives very weak room temperature emission at 603 nm and 630 nm respectively. | Keywords/Search Tags: | Metalloprotein, Room temperature emission, 4-helix bundle, Random coil, Hydrophobic, Exists, Peptide | | Related items |
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