Non-Sequence-Specific Interactions Can Account for the Compaction of Proteins Unfolded under "Native" Conditions

Journal of Molecular Biology

Volumn 394, Issue 2, 2009, Pages 343-350

  Kohn, Jonathan E ^a   Gillespie, Blake ^b   Plaxco, Kevin W ^c  

^a University of California at Berkeley   (United States)

^b CALIFORNIA STATE UNIVERSITY CHANNEL ISLANDS   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

folding kinetics; guanidine hydrochloride; natively unfolded; residual structure

Indexed keywords

GLOBULAR PROTEIN; POLYPEPTIDE; PROTEIN KINASE FYN; SOLVENT;

AMINO ACID COMPOSITION; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; HYDRODYNAMICS; MOLECULAR INTERACTION; MUTATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING;

EID: 70350532228     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.09.005     Document Type: Article

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