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Parallel β-sheet secondary structure is stabilized and terminated by interstrand disulfide cross-linking.
Sat, 12/01/2012 - 8:52am — ldowdall
| Title | Parallel β-sheet secondary structure is stabilized and terminated by interstrand disulfide cross-linking. |
| Publication Type | Journal Article |
| Year of Publication | 2012 |
| Authors | Almeida, AM, Li, R, Gellman, SH |
| Journal | J Am Chem Soc |
| Volume | 134 |
| Issue | 1 |
| Pagination | 75-8 |
| Date Published | 2012 Jan 11 |
| ISSN | 1520-5126 |
| Keywords | disulfides, Magnetic Resonance Spectroscopy, Models, Molecular, peptides, protein stability, Protein Structure, Secondary |
| Abstract | Disulfide bonds between Cys residues in adjacent strands of parallel β-sheets are rare among proteins, which suggests that parallel β-sheet structure is not stabilized by such disulfide cross-links. We report experimental results that show, surprisingly, that an interstrand disulfide bond can stabilize parallel β-sheets formed by an autonomously folding peptide in aqueous solution. NMR analysis reveals that parallel β-sheet structure is terminated beyond the disulfide bond, which causes deviation from the extended backbone conformation at one of the Cys residues. |
| DOI | 10.1021/ja208856c |
| Custom 1 | |
| Alternate Journal | J. Am. Chem. Soc. |
| PubMed ID | 22148521 |
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