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Lack of coupling between secondary structure formation and collapse in a model polypeptide that mimics early folding intermediates, the F2 fragment of the Escherichia coli tryptophan-synthase beta chain.
The isolated, 101-residue long C-terminal (so called F2) fragment of the beta chain from Escherichia coli tryptophan synthase was shown previously to fold into an ensemble of conformations that are condensed, to contain large amounts of highly dynamic secondary structures, and to behave as a good mo...
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| Main Authors: | , , , , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Cold Spring Harbor Laboratory Press
1997
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2143624/ https://ncbi.nlm.nih.gov/pubmed/9416607 |
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