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Thermodynamic characterization of an artificially designed amphiphilic alpha-helical peptide containing periodic prolines: observations of high thermal stability and cold denaturation.
To investigate the structural stability of proteins, we analyzed the thermodynamics of an artificially designed 30-residue peptide. The designed peptide, NH2-EELLPLAEALAPLLEALLPLAEALAPLLKK-COOH (PERI COIL-1), with prolines at i + 7 positions, forms a pentameric alpha-helical structure in aqueous sol...
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| Autores principales: | , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
Cold Spring Harbor Laboratory Press
1994
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2142719/ https://ncbi.nlm.nih.gov/pubmed/8061612 |
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