Conformation of a T cell stimulating peptide in aqueous solution
Using two‐dimensional NMR spectroscopy and circular dichroism spectroscopy it is demonstrated that a T cell stimulating peptide corresponding to residues 132–153 of sperm whale myoglobin populates helical conformations in aqueous solution. This finding is in accordance with proposals that immunodomi...
| Published in: | FEBS Letters |
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| Main Authors: | , , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
1989
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1016/0014-5793(89)80764-1 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2F0014-5793%2889%2980764-1 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2F0014-5793(89)80764-1 https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2889%2980764-1 |
| Summary: | Using two‐dimensional NMR spectroscopy and circular dichroism spectroscopy it is demonstrated that a T cell stimulating peptide corresponding to residues 132–153 of sperm whale myoglobin populates helical conformations in aqueous solution. This finding is in accordance with proposals that immunodominant sites in T cell stimulating peptides have a high conformational propensity. The observation of secondary structure in aqueous solutions of this and other immunogenic peptides has important implications for initiation of protein folding. |
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