Intermolecular aggregations are responsible for the slow kinetics observed in the folding of cytochrome c at neutral pH

Journal of Molecular Biology

Volumn 293, Issue 5, 1999, Pages 991-995

  Nawrocki, Joseph P ^a   Chu, Rui Ai ^b   Pannell, Lewis K ^a   Bai, Yawen ^b  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b NATIONAL CANCER INSTITUTE   (United States)

Author keywords

2H H exchange pulse labeling; Cytochrome c; Intermolecular aggregation; Protein folding; Protein folding pathway

Indexed keywords

CYTOCHROME C;

ARTICLE; CONTROLLED STUDY; ISOTOPE LABELING; NUCLEAR MAGNETIC RESONANCE; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING;

EQUIDAE;

EID: 0033550201     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3226     Document Type: Article

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