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Designed tail peptides change overall GFP properties


Research in small folding peptides has produced several examples which rely on "natural" folds [1-3].
These appear to be degraded in our lab in E. coli if they are expressed as GFP tails.
We have designed and made examples of "artificial" peptides with unique folds which are easily expressed as GFP fusions.
Two types of tags indicate unusual peptide interactions or folding:
-Terminal His-Gly-His binds tightly to IMAC resin (like His6).
-Two histidines separated by multiple amino acids bind to IMAC if the amino acids fold to bring the His together to chelate the metal.
High IMAC affinity assures tails with terminal HGH are intact (and not degraded in vivo.)

A new fold relies on a central arginine hydrogen bonded to the main chain amides, and hold aromatic groups in close proximity.

Rigid proline-rich peptides have novel binding properties.

[1]  D. Satoh, K. Shimizu, S. Nakamura, T. Terada, Folding free-energy landscape of a 10-residue mini-protein, chignolin. FEBS Lett. 580:3422 (2006).
[2] A.G. Cochran, N.J. Skelton, M.A. Starovasnik, Tryptophan zippers: Stable, monomeric beta-hairpins. Proc. Natl Acad. Sci. 98:5578 (2001).
[3] N.H. Anderson, K.A. Olsen, R.M. Fesinmeyer, X. Tan, F.M. Hudson, L.A. Eidenschink, S.R. Farazi, Minimization and optimization of designed beta-hairpin folds. J. Am. Chem. Soc. 128:6101 (2006).