Structural correspondence between the α-helix and the random-flight chain resolves how unfolded proteins can have native-like properties

Nature Structural Biology

Volumn 10, Issue 11, 2003, Pages 955-961

  Zagrovic, Bojan ^a   Pande, Vijay S ^a  

^a STANFORD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

ALPHA HELIX; ARTICLE; DISTANCE PERCEPTION; MATHEMATICAL COMPUTING; MATHEMATICAL MODEL; MEAN STRUCTURE HYPOTHESIS; OPTICAL RESOLUTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; RANDOM FLIGHT CHAIN; ROOM TEMPERATURE; SIMULATION; STATISTICAL ANALYSIS; STRUCTURE ACTIVITY RELATION;

COMPUTER SIMULATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; STAPHYLOCOCCAL PROTEIN A;

EID: 0242407127     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb995     Document Type: Article

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