A comparison of the folding kinetics of a small, artificially selected DNA aptamer with those of equivalently simple naturally occurring proteins

Protein Science

Volumn 23, Issue 1, 2014, Pages 56-66

  Lawrence, Camille ^a   Vallée Bélisle, Alexis ^a,b   Pfeil, Shawn H ^a,c   De Mornay, Derek ^a   Lipman, Everett A ^a   Plaxco, Kevin W ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITÉ DE MONTRÉAL   (Canada)

^c WEST CHESTER UNIVERSITY   (United States)

Author keywords

Chevron; Contact order; Ionic strength; Phi ( ); Single molecule F rster resonance energy transfer (FRET); Tanford beta ( ); Topomer search

Indexed keywords

APTAMER; UREA;

ARTICLE; FLUORESCENCE RESONANCE ENERGY TRANSFER; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

CHEVRON; CONTACT ORDER; IONIC STRENGTH; PHI (Φ); SINGLE MOLECULE FÖRSTER RESONANCE ENERGY TRANSFER (FRET); TANFORD BETA (Β); TOPOMER SEARCH;

APTAMERS, NUCLEOTIDE; FLUORESCENCE RESONANCE ENERGY TRANSFER; KINETICS; MODELS, MOLECULAR; NUCLEIC ACID CONFORMATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEINS; THERMODYNAMICS;

EID: 84900390627     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2390     Document Type: Article

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