Direct observation of ultrafast folding and denatured state dynamics in single protein molecules

scientific article published on 19 October 2009

Direct observation of ultrafast folding and denatured state dynamics in single protein molecules is …
instance of (P31):
scholarly articleQ13442814

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P819ADS bibcode2009PNAS..10618569N
P356DOI10.1073/PNAS.0910860106
P932PMC publication ID2773960
P698PubMed publication ID19841261
P5875ResearchGate publication ID38022309

P50authorAlan FershtQ537479
P2093author name stringChristopher M Johnson
Hannes Neuweiler
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A microscopic view of miniprotein folding: enhanced folding efficiency through formation of an intermediateQ33226561
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Direct observation of barrier-limited folding of BBL by single-molecule fluorescence resonance energy transferQ33508761
The protein folding 'speed limit'.Q34315486
Biological and chemical applications of fluorescence correlation spectroscopy: a reviewQ34492569
Protein folding and unfolding at atomic resolutionQ34574339
Sorting single molecules: application to diagnostics and evolutionary biotechnologyQ34719523
Protein folding studied by single-molecule FRET.Q34742014
Ultrafast dynamics of protein collapse from single-molecule photon statistics.Q35669661
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Single-molecule protein folding: diffusion fluorescence resonance energy transfer studies of the denaturation of chymotrypsin inhibitor 2Q36966513
P433issue44
P407language of work or nameEnglishQ1860
P921main subjectprotein foldingQ847556
P1104number of pages6
P304page(s)18569-18574
P577publication date2009-10-19
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleDirect observation of ultrafast folding and denatured state dynamics in single protein molecules
P478volume106

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