A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native β-hairpin

@article{Searle1995ASL,
  title={A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native β-hairpin},
  author={M. S. Searle and Daniel Williams and Leonard C. Packman},
  journal={Nature Structural Biology},
  year={1995},
  volume={2},
  pages={999-1006}
}
  • M. S. Searle, Daniel Williams, Leonard C. Packman
  • Published in Nature Structural Biology 1995
  • Chemistry, Medicine
  • A 16-residue peptide derived from the N-terminal sequence of ubiquitin forms a stable monomeric β-hairpin that is estimated to be ∼80% populated in aqueous solution. The peptide sequence has been modified from native ubiquitin by replacing the five residues found in a type IG1 bulged turn (Thr-Leu-Thr-Gly-Lys) with four residues (Asn-Pro-Asp-Gly) to maximize the probability of forming a β-turn. Unexpectedly, the bulged turn conformation is re-established in the β-hairpin in solution with two… CONTINUE READING

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