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- W2092509527 endingPage "983" @default.
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- W2092509527 abstract "A class of regulators of eukaryotic gene expression contains a conserved amino acid sequence responsible for protein oligomerization and binding to DNA. This structure consists of an arginine- and lysine-rich basic region followed by a helix-loop-helix motif, which together mediate specific binding to DNA. Peptides were prepared that span this motif in the MyoD protein; in solution, they formed α-helical dimers and tetramers. They bound to DNA as dimers and their α-helical content increased on binding. Parallel and antiparallel four-helix models of the DNA-bound dimer were constructed. Peptides containing disulfide bonds were engineered to test the correctness of the two models. A disulfide that is compatible with the parallel model promotes specific interaction with DNA, whereas a disulfide compatible with the antiparallel model abolishes specific binding. Electron paramagnetic resonance (EPR) measurements of nitroxide-labeled peptides provided intersubunit distance measurements that also supported the parallel model." @default.
- W2092509527 created "2016-06-24" @default.
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- W2092509527 date "1992-02-21" @default.
- W2092509527 modified "2023-10-11" @default.
- W2092509527 title "Molecular Characterization of Helix-Loop-Helix Peptides" @default.
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- W2092509527 doi "https://doi.org/10.1126/science.1312255" @default.
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