Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time

scientific article

Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1021/BI9829433
P698PubMed publication ID10194334

P2093author name stringL Yang
C R Matthews
O Bilsel
J M Beechem
J A Zitzewitz
P433issue13
P407language of work or nameEnglishQ1860
P921main subjectrefoldingQ3935998
P304page(s)4177-4187
P577publication date1999-03-01
P1433published inBiochemistryQ764876
P1476titleTime-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time
P478volume38

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cites work (P2860)
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Q44247940Fluorescence and folding properties of Tyr mutant tryptophan synthase alpha-subunits from Escherichia coli
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Q36281564Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein
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