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Volumn 3, Issue , 2013, Pages

Microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 84881336284     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep02151     Document Type: Article
Times cited : (26)

References (16)
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    • Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
    • DOI 10.1038/nature01060
    • Schuler, B., Lipman, E. A. & Eaton, W. A. Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy. Nature 419, 743-747 (2002). (Pubitemid 35177962)
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    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3
  • 7
    • 84863963784 scopus 로고    scopus 로고
    • Long-term observation of fluorescence of free single molecules to explore protein-folding energy landscapes
    • Kamagata, K. et al. Long-term observation of fluorescence of free single molecules to explore protein-folding energy landscapes. J. Am. Chem. Soc. 134, 11525-11532 (2012).
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    • Kamagata, K.1
  • 8
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    • A photoprotection strategy for microsecond-resolution single-molecule fluorescence spectroscopy
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    • Campos, L.A.1
  • 9
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    • Single molecule fluorescence under conditions of fast flow
    • Horrocks, M. H. et al. Single molecule fluorescence under conditions of fast flow. Anal. Chem. 84, 179-185 (2012).
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    • Horrocks, M.H.1
  • 12
    • 65249086776 scopus 로고    scopus 로고
    • Time-resolved fluorescence resonance energy transfer study shows a compact denatured state of the b domain of protein a
    • Huang, F. et al. Time-resolved fluorescence resonance energy transfer study shows a compact denatured state of the B domain of protein A. Biochemistry 48, 3468-3476 (2009).
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    • Huang, F.1
  • 14
    • 77957937199 scopus 로고    scopus 로고
    • Atomic-level characterization of the structural dynamics of proteins
    • Shaw, D. E. et al. Atomic-level characterization of the structural dynamics of proteins. Science 330, 341-346 (2010).
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    • A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase from escherichia coli
    • Iwakura, M., Jones, B. E., Luo, J. & Matthews, C. R. A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase from Escherichia coli. J. Biochem. 117, 480-488 (1995).
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    • Iwakura, M.1    Jones, B.E.2    Luo, J.3    Matthews, C.R.4
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.