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Defining the minimum size of a hydrophobic cluster in two-stranded α-helical coiled-coils: Effects on protein stability
The α-helical coiled-coil motif is characterized by a heptad repeat pattern (abcdefg)(n) in which residues a and d form the hydrophobic core. Long coiled-coils (e.g., tropomyosin, 284 residues per polypeptide chain) typically do not have a continuous hydrophobic core of stabilizing residues, but rat...
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| Main Authors: | , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
Cold Spring Harbor Laboratory Press
2004
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| Acceso en liña: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2286740/ https://ncbi.nlm.nih.gov/pubmed/14978309 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.03443204 |
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