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. Author manuscript; available in PMC: 2012 May 31.
Published in final edited form as: Biochemistry. 2011 May 3;50(21):4741–4749. doi: 10.1021/bi200585n

Figure 2.

Figure 2

Varying presentations of the tripeptide substrate to DNA in the open architecture. (A) Presentation with a short three-carbon tether linking the DNA anchor to the CXA tripeptide via a disulfide bond, illustrated with X = Tyr, i.e., CYA tripeptide. The initially random pool is N40, and the loop on the right side is present only during the selection process. (B) Presentation with a longer hexa(ethylene glycol) (HEG) tether to the CYA tripeptide. (C) Presentation with untethered free CYA tripeptide and a DNA helper oligonucleotide in place of the DNA anchor. In all cases, the N-acetyl group on the amino terminus of the tripeptide was included to suppress potential amine nucleophilicity.

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