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How strong are side chain interactions in the folding intermediate?
Influence of 12 nonpolar amino acids residues from the hydrophobic core of apomyoglobin on stability of its native state and folding intermediate was studied. Six of the selected residues are from the A, G and H helices; these are conserved in structure of the globin family, although nonfunctional,...
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| Autores principales: | , , , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
Wiley Subscription Services, Inc., A Wiley Company
2009
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2786978/ https://ncbi.nlm.nih.gov/pubmed/19693934 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.229 |
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