Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure

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

Volumn 110, Issue 6, 2013, Pages 2123-2128

  Meng, Wenli ^a   Lyle, Nicholas ^b   Luan, Bowu ^a   Raleigh, Daniel P ^a   Pappu, Rohit V ^b  

^a STONY BROOK UNIVERSITY   (United States)

^b WASHINGTON UNIVERSITY IN ST LOUIS   (United States)

Author keywords

Atomistic simulations; Denatured proteins; Paramagnetic relaxation

Indexed keywords

N TERMINAL DOMAIN OF L9; RIBOSOME PROTEIN; UNCLASSIFIED DRUG; UREA;

ARTICLE; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN UNFOLDING;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BIOPHYSICAL PHENOMENA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN UNFOLDING; RIBOSOMAL PROTEINS; SCATTERING, SMALL ANGLE; SEQUENCE HOMOLOGY, AMINO ACID; UREA; X-RAY DIFFRACTION;

EID: 84873441997     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1216979110     Document Type: Article

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