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Domain‐Specific Folding Kinetics of Staphylococcal Nuclease Observed through Single‐Molecule FRET in a Microfluidic Mixer
Author(s) -
Zhi Zeyong,
Liu Pengcheng,
Wang Peng,
Huang Yanyi,
Zhao Xin Sheng
Publication year - 2011
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201100652
Subject(s) - förster resonance energy transfer , single molecule fret , folding (dsp implementation) , chemistry , biophysics , kinetics , nuclease , microfluidics , molecule , single molecule experiment , fluorescence , protein folding , crystallography , nanotechnology , materials science , biochemistry , dna , biology , physics , organic chemistry , quantum mechanics , electrical engineering , engineering
Fast Folding: A combined single‐molecule fluorescence resonance energy transfer (smFRET) and microfluidic mixing study reveals that the α‐helical subdomain of staphylococcal nuclease (SNase) (see picture) folds about ten times faster than the β‐sheet subdomain.