Gradual disordering of the native state on a slow two-state folding protein monitored by single-molecule fluorescence spectroscopy and NMR

Journal of Physical Chemistry B

Volumn 117, Issue 42, 2013, Pages 13120-13131

  Campos, Luis A ^a,b,c   Sadqi, Mourad ^a,b,c   Liu, Jianwei ^b,d   Wang, Xiang ^b,e   English, Douglas S ^b,f   Muñoz, Victor ^a,b,c  

^a CENTRO DE INVESTIGACIONES BIOLÓGICAS   (Spain)

^b Bldg 142   (United States)

^c CENTRO NACIONAL DE BIOTECNOLOGÍA   (Spain)

^d FUDAN UNIVERSITY   (China)

^e UNIVERSITY OF COLORADO   (United States)

^f WICHITA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENCE SPECTROSCOPY; FORSTER RESONANCE ENERGY TRANSFER; FREE ENERGY; HYDROGEN BONDS; MOLECULES;

DENATURING CONDITIONS; FOLDING TRANSITION STATE; FREE ENERGY LANDSCAPE; INTRA-MOLECULAR HYDROGEN BONDS; LINEAR EXTRAPOLATION; PHYSIOLOGICAL CONDITION; SINGLE-MOLECULE FLUORESCENCE SPECTROSCOPY; THERMAL UNFOLDING TRANSITIONS;

PROTEINS;

FLUORESCENT DYE; RECOMBINANT PROTEIN; SPECTRIN;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BIOSYNTHESIS; CHEMISTRY; CHICKEN; GENETICS; HYDROGEN BOND; METABOLISM; MOLECULAR GENETICS; MUTATION; NUCLEAR MAGNETIC RESONANCE; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROFLUOROMETRY; SRC HOMOLOGY DOMAIN; TEMPERATURE;

AMINO ACID SEQUENCE; ANIMALS; CHICKENS; FLUORESCENT DYES; HYDROGEN BONDING; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SPECTRIN; SPECTROMETRY, FLUORESCENCE; SRC HOMOLOGY DOMAINS; TEMPERATURE;

EID: 84886644051     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp403051k     Document Type: Article

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