Single-molecule fluorescence spectroscopy maps the folding landscape of a large protein

scientific article published on 11 October 2011

Single-molecule fluorescence spectroscopy maps the folding landscape of a large protein is …
instance of (P31):
scholarly articleQ13442814

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P819ADS bibcode2011NatCo...2..493P
P6179Dimensions Publication ID1033447566
P356DOI10.1038/NCOMMS1504
P2888exact matchhttps://scigraph.springernature.com/pub.10.1038/ncomms1504
P932PMC publication ID3209527
P698PubMed publication ID21988909
P5875ResearchGate publication ID51708642

P50authorGuy ZivQ53843497
Nir ZoharQ56971655
P2093author name stringYoav Barak
Guy Ziv
Gilad Haran
Inbal Riven
Menahem Pirchi
Sharona Sedghani Cohen
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Noncooperative folding of subdomains in adenylate kinaseQ34945858
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The natively helical chain segment 169-188 of Escherichia coli adenylate kinase is formed in the latest phase of the refolding transitionQ44070157
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The foldon universe: a survey of structural similarity and self-recognition of independently folding units 1 1Edited by F. E. CohenQ57971790
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Protein Folding and Dynamics from Optical Single Molecule SpectroscopyQ59332543
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Symmetric connectivity of secondary structure elements enhances the diversity of folding pathwaysQ81340111
P407language of work or nameEnglishQ1860
P921main subjectspectroscopyQ483666
protein foldingQ847556
fluorescence spectroscopyQ1768467
P304page(s)493
P577publication date2011-10-11
P1433published inNature CommunicationsQ573880
P1476titleSingle-molecule fluorescence spectroscopy maps the folding landscape of a large protein
P478volume2

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