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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Autori principali: Visser, Nina V., Westphal, Adrie H., van Hoek, Arie, van Mierlo, Carlo P. M., Visser, Antonie J. W. G., van Amerongen, Herbert
Natura: Artigo
Lingua:Inglês
Pubblicazione: The Biophysical Society 2008
Soggetti:
Proteins
Accesso online: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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