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Folding of beta pep-4 beta-sheet sandwich dimers and tetramers is influenced by aliphatic hydrophobic residues at the intersubunit interface.
For the designed peptide 33mer, beta pep-4, formation of beta-sheet structure [Ilyina, Roongta and Mayo (1997) Biochemistry 36, 5245--5250] is thermodynamically linked to self-association. Dimers and tetramers are stabilized by interactions between hydrophobic residues lying on the hydrophobic faces...
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| Main Authors: | , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2001
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1222003/ https://ncbi.nlm.nih.gov/pubmed/11463344 |
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