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Synthetic Approach to Study the Effects of β-Turn Residues on the Structure and Folding of Bovine Pancreatic Trypsin Inhibitor (BPTI)

  • Judit Tulla
  • Clare Woodward
  • George Barany
Part of the American Peptide Symposia book series (APSY, volume 7)

Abstract

Previous work from our laboratory has established a system for accessing partially folded conformational ensembles of bovine pancreatic trypsin inhibitor (BPTI), based on the replacement of Cys 5, 30, 51, and 55 by α-amino-n-butyric acid (Abu), while retaining the disulfide between Cys 14 and 38 [1]. Several observations in the aforementioned [14–38]Abu system suggest that the type I β-turn (A25K26A27G28) connecting the two core strands of the antiparallel β-sheet (residues 18–24 and 29–35) is the main site for initiation of folding of BPTI [2], For the present work, two analogues of [14–38]Abu have been synthesized in which turn residues at positions 26, 27, and 28 were altered to maximize amino acid positional potentials for β-turns [3]. One analogue, P26, D27[14–38]Abu, has at three positions (including the natural G28) residues with the highest potential for a type I β-turn. In a second analogue, N26,G27,K28[14–38]Abu, residues with the highest potential for a type I′ β-turn have been introduced. Type I′ β-turns are most common for β-hairpins [4].

Keywords

Parent Protein Conformational Ensemble Bovine Pancreatic Trypsin Inhibitor Strong Minimum Negative Ellipticity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media Dordrecht 2001

Authors and Affiliations

  • Judit Tulla
    • 1
  • Clare Woodward
    • 2
  • George Barany
    • 1
  1. 1.Department of ChemistryUniversity of MinnesotaMinneapolisUSA
  2. 2.Department of Biochemistry, Molecular Biology, and BiophysicsUniversity of MinnesotaSt. PaulUSA

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