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Pressure-induced structural rearrangements of bovine pancreatic trypsin inhibitor studied by FTIR spectroscopy

1998; Wiley; Volume: 4; Issue: 3 Linguagem: Inglês

10.1002/(sici)1520-6343(1998)4

1520-6343

Naohiro Takeda, Kayoko Nakano, Minoru Katō, Yoshihiro Taniguchi,

Mass Spectrometry Techniques and Applications

BiospectroscopyVolume 4, Issue 3 p. 209-216 Pressure-induced structural rearrangements of bovine pancreatic trypsin inhibitor studied by FTIR spectroscopy Naohiro Takeda, Naohiro Takeda Department of Chemistry, Faculty of Science and Engineering, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, JapanSearch for more papers by this authorKayoko Nakano, Kayoko Nakano Department of Chemistry, Faculty of Science and Engineering, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, JapanSearch for more papers by this authorMinoru Kato, Minoru Kato Department of Chemistry, Faculty of Science and Engineering, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, JapanSearch for more papers by this authorYoshihiro Taniguchi, Corresponding Author Yoshihiro Taniguchi taniguti@se.ritsumei.ac.jp Department of Chemistry, Faculty of Science and Engineering, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, JapanDepartment of Chemistry, Faculty of Science and Engineering, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, JapanSearch for more papers by this author Naohiro Takeda, Naohiro Takeda Department of Chemistry, Faculty of Science and Engineering, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, JapanSearch for more papers by this authorKayoko Nakano, Kayoko Nakano Department of Chemistry, Faculty of Science and Engineering, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, JapanSearch for more papers by this authorMinoru Kato, Minoru Kato Department of Chemistry, Faculty of Science and Engineering, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, JapanSearch for more papers by this authorYoshihiro Taniguchi, Corresponding Author Yoshihiro Taniguchi taniguti@se.ritsumei.ac.jp Department of Chemistry, Faculty of Science and Engineering, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, JapanDepartment of Chemistry, Faculty of Science and Engineering, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, JapanSearch for more papers by this author First published: 07 December 1998 https://doi.org/10.1002/(SICI)1520-6343(1998)4:3 3.0.CO;2-ZCitations: 13AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract Fourier transform infrared (FTIR) spectroscopy combined with resolution enhancement techniques, second-derivative and difference spectroscopies, have been used to characterize pressure-induced changes in the structural rearrangements of bovine pancreatic trypsin inhibitor (BPTI) in D2O solution at 25.0°C. According to the observed changes in the amide I′ band up to 550 MPa, the secondary structure elements of BPTI, such as the α-helix, 310-helix, β-sheet, and β-turn, are scarcely rearranged except for the loop structure of residues of 9–17 and 36–43. The polypeptide backbone is not extensively unfolded up to 550 MPa. The minor pressure-induced structural rearrangements are completely reversible. A further increase in pressure above 1000 MPa associated with the precipitation of BPTI in D2O buffer solution induces the partial structural rearrangements of the α-helix, β-turn and/or 310-helix, and β-sheet. The polypeptide backbone of BPTI is not fully unfolded even above 1000 MPa. Most of the protected backbone amide protons involved in the β-sheet remain intact in the pressure range where BPTI is not precipitated, while those involved in the α-helix and β-turn and/or 310-helix are exchanged with solvent deuterons. The protected backbone amide protons located near the surface regions are more easily exchanged with solvent deuterons by application of high pressure than those involved in the core. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 209–216, 1998 Citing Literature Volume4, Issue31998Pages 209-216 RelatedInformation