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)


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].


Parent Protein Conformational Ensemble Bovine Pancreatic Trypsin Inhibitor Strong Minimum Negative Ellipticity 
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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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