Thermodynamic analysis of the disorder-to-α-helical transition of 18.5-kDa myelin basic protein reveals an equilibrium intermediate representing the most compact conformation

Journal of Molecular Biology

Volumn 427, Issue 10, 2015, Pages 1977-1992

  Vassall, Kenrick A ^a   Jenkins, Andrew D ^a   Bamm, Vladimir V ^a   Harauz, George ^a  

^a UNIVERSITY OF GUELPH   (Canada)

Author keywords

F rster (fluorescence) resonance energy transfer (FRET); intrinsically disordered protein; molecular recognition fragment (MoRF); myelin basic protein (MBP); protein folding intermediate

Indexed keywords

1-ANILINO-8-NAPHTHALENESULFONATE; 8 ANILINO 1 NAPHTHALENESULFONIC ACID; MUTANT PROTEIN; MYELIN BASIC PROTEIN; PEPTIDE FRAGMENT; PROTEIN BINDING; RECOMBINANT PROTEIN;

CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; FLUORESCENCE RESONANCE ENERGY TRANSFER; GENETICS; HUMAN; METABOLISM; MUTATION; PROTEIN CONFORMATION; THERMODYNAMICS;

ANILINO NAPHTHALENESULFONATES; CIRCULAR DICHROISM; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMANS; MODELS, MOLECULAR; MUTANT PROTEINS; MUTATION; MYELIN BASIC PROTEIN; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; THERMODYNAMICS;

EID: 84937738009     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2015.03.011     Document Type: Article

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