Folding of a heterogeneous β-hairpin peptide from temperature-jump 2D IR spectroscopy
We provide a time- and structure-resolved characterization of the folding of the heterogeneous β-hairpin peptide Tryptophan Zipper 2 (Trpzip2) using 2D IR spectroscopy. The amide I′ vibrations of three Trpzip2 isotopologues are used as a local probe of the midstrand contacts, β-turn, and overall β-s...
| Main Authors: | , , |
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| Other Authors: | |
| Format: | Article |
| Language: | en_US |
| Published: |
National Academy of Sciences (U.S.)
2013
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| Online Access: | http://hdl.handle.net/1721.1/80379 |
| _version_ | 1826193955391275008 |
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| author | Jones, Kevin C. Peng, C. S. Tokmakoff, A. |
| author2 | Massachusetts Institute of Technology. Department of Chemistry |
| author_facet | Massachusetts Institute of Technology. Department of Chemistry Jones, Kevin C. Peng, C. S. Tokmakoff, A. |
| author_sort | Jones, Kevin C. |
| collection | MIT |
| description | We provide a time- and structure-resolved characterization of the folding of the heterogeneous β-hairpin peptide Tryptophan Zipper 2 (Trpzip2) using 2D IR spectroscopy. The amide I′ vibrations of three Trpzip2 isotopologues are used as a local probe of the midstrand contacts, β-turn, and overall β-sheet content. Our experiments distinguish between a folded state with a type I′ β-turn and a misfolded state with a bulged turn, providing evidence for distinct conformations of the peptide backbone. Transient 2D IR spectroscopy at 45 °C following a laser temperature jump tracks the nanosecond and microsecond kinetics of unfolding and the exchange between conformers. Hydrogen bonds to the peptide backbone are loosened rapidly compared with the 5-ns temperature jump. Subsequently, all relaxation kinetics are characterized by an observed 1.2 ± 0.2-μs exponential. Our time-dependent 2D IR spectra are explained in terms of folding of either native or nonnative contacts from a common compact disordered state. Conversion from the disordered state to the folded state is consistent with a zip-out folding mechanism. |
| first_indexed | 2024-09-23T09:47:35Z |
| format | Article |
| id | mit-1721.1/80379 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T09:47:35Z |
| publishDate | 2013 |
| publisher | National Academy of Sciences (U.S.) |
| record_format | dspace |
| spelling | mit-1721.1/803792022-09-26T13:46:59Z Folding of a heterogeneous β-hairpin peptide from temperature-jump 2D IR spectroscopy Jones, Kevin C. Peng, C. S. Tokmakoff, A. Massachusetts Institute of Technology. Department of Chemistry Jones, Kevin C. Tokmakoff, A. Peng, C. S. We provide a time- and structure-resolved characterization of the folding of the heterogeneous β-hairpin peptide Tryptophan Zipper 2 (Trpzip2) using 2D IR spectroscopy. The amide I′ vibrations of three Trpzip2 isotopologues are used as a local probe of the midstrand contacts, β-turn, and overall β-sheet content. Our experiments distinguish between a folded state with a type I′ β-turn and a misfolded state with a bulged turn, providing evidence for distinct conformations of the peptide backbone. Transient 2D IR spectroscopy at 45 °C following a laser temperature jump tracks the nanosecond and microsecond kinetics of unfolding and the exchange between conformers. Hydrogen bonds to the peptide backbone are loosened rapidly compared with the 5-ns temperature jump. Subsequently, all relaxation kinetics are characterized by an observed 1.2 ± 0.2-μs exponential. Our time-dependent 2D IR spectra are explained in terms of folding of either native or nonnative contacts from a common compact disordered state. Conversion from the disordered state to the folded state is consistent with a zip-out folding mechanism. National Science Foundation (U.S.) (Grant CHE-0616575) National Science Foundation (U.S.) (Grant CHE-0911107) 2013-09-09T18:22:22Z 2013-09-09T18:22:22Z 2013-02 2012-07 Article http://purl.org/eprint/type/JournalArticle 0027-8424 1091-6490 http://hdl.handle.net/1721.1/80379 Jones, K. C., C. S. Peng, and A. Tokmakoff. “Folding of a heterogeneous -hairpin peptide from temperature-jump 2D IR spectroscopy.” Proceedings of the National Academy of Sciences 110, no. 8 (February 19, 2013): 2828-2833. en_US http://dx.doi.org/10.1073/pnas.1211968110 Proceedings of the National Academy of Sciences Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf National Academy of Sciences (U.S.) PNAS |
| spellingShingle | Jones, Kevin C. Peng, C. S. Tokmakoff, A. Folding of a heterogeneous β-hairpin peptide from temperature-jump 2D IR spectroscopy |
| title | Folding of a heterogeneous β-hairpin peptide from temperature-jump 2D IR spectroscopy |
| title_full | Folding of a heterogeneous β-hairpin peptide from temperature-jump 2D IR spectroscopy |
| title_fullStr | Folding of a heterogeneous β-hairpin peptide from temperature-jump 2D IR spectroscopy |
| title_full_unstemmed | Folding of a heterogeneous β-hairpin peptide from temperature-jump 2D IR spectroscopy |
| title_short | Folding of a heterogeneous β-hairpin peptide from temperature-jump 2D IR spectroscopy |
| title_sort | folding of a heterogeneous β hairpin peptide from temperature jump 2d ir spectroscopy |
| url | http://hdl.handle.net/1721.1/80379 |
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