Influence of local and residual structures on the scaling behavior and dimensions of unfolded proteins

Biopolymers

Volumn 86, Issue 4, 2007, Pages 321-328

  Wang, Zhisong ^a,b   Plaxco, Kevin W ^c   Makarov, Dmitrii E ^b  

^a FUDAN UNIVERSITY   (China)

^b UNIVERSITY OF TEXAS AT AUSTIN   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

helix; Monte Carlo simulation; PPII helix; Random coil; Unfolded proteins

Indexed keywords

POLYPROLINE II (PPII) HELIX; RANDOM COIL; UNFOLDED PROTEINS;

COMPUTER SIMULATION; DENATURATION; METHANOL; MONTE CARLO METHODS; SCALING LAWS; X RAY SCATTERING;

PROTEINS;

PROTEIN;

ALPHA HELIX; ARTICLE; MONTE CARLO METHOD; PROTEIN FOLDING; PROTEIN STRUCTURE;

COMPUTER SIMULATION; METHANOL; MODELS, BIOLOGICAL; PEPTIDES; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; UREA;

EID: 34447578997     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.20747     Document Type: Article

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