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Alteration of the disulfide-coupled folding pathway of BPTI by circular permutation
The kinetics of disulfide-coupled folding and unfolding of four circularly permuted forms of bovine pancreatic trypsin inhibitor (BPTI) were studied and compared with previously published results for both wild-type BPTI and a cyclized form. Each of the permuted proteins was found to be less stable t...
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| Main Authors: | , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Cold Spring Harbor Laboratory Press
2004
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2286756/ https://ncbi.nlm.nih.gov/pubmed/15096625 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.03563704 |
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