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Tryptophan-Tryptophan Energy Migration as a Tool to Follow Apoflavodoxin Folding
Submolecular details of Azotobacter vinelandii apoflavodoxin (apoFD) (un)folding are revealed by time-resolved fluorescence anisotropy using wild-type protein and variants lacking one or two of apoFD's three tryptophans. ApoFD equilibrium (un)folding by guanidine hydrochloride follows a three-s...
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| Hoofdauteurs: | , , , , , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
The Biophysical Society
2008
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2517029/ https://ncbi.nlm.nih.gov/pubmed/18708472 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1529/biophysj.108.132001 |
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