Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments

Proceedings of the National Academy of Sciences of the United States of America

Volumn 111, Issue 13, 2014, Pages 4874-4879

  Soranno, Andrea ^a   Koenig, Iwo ^a   Borgia, Madeleine B ^a   Hofmann, Hagen ^a   Zosel, Franziska ^a   Nettels, Daniel ^a   Schuler, Benjamin ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

Excluded volume screening; Flory Huggins theory; Single molecule FRET; Unfolded state collapse

Indexed keywords

INTEGRASE; INTRINSICALLY DISORDERED PROTEIN; POLYMER; POLYPEPTIDE; PROTHYMOSIN ALPHA; VIRUS ENZYME;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATION; ENERGY TRANSFER; HUMAN; MOLECULAR CROWDING; MOLECULAR WEIGHT; NONHUMAN; PHASE TRANSITION; POLYMERIZATION; PRIORITY JOURNAL; SINGLE MOLECULE SPECTROSCOPY; SPECTROSCOPY;

EXCLUDED VOLUME SCREENING; FLORY-HUGGINS THEORY; SINGLE-MOLECULE FRET; UNFOLDED STATE COLLAPSE;

AMINO ACID SEQUENCE; BIOPOLYMERS; FLUORESCENCE RESONANCE ENERGY TRANSFER; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; INTRINSICALLY DISORDERED PROTEINS; MACROMOLECULAR SUBSTANCES; MOLECULAR WEIGHT; PROTEIN BINDING; SOLUTIONS; SPECTRUM ANALYSIS;

EID: 84897513201     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1322611111     Document Type: Article

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