An aggregation-prone intermediate species is present in the unfolding pathway of the monomeric portal protein of bacteriophage P22: Implications for portal assembly

Biochemistry

Volumn 46, Issue 25, 2007, Pages 7353-7364

  Braga, Carolina A C A ^a   Carvalho, Danielle ^a   Lara, Flávio Alves ^a   Cortines, Juliana Reis ^a,b   Moore, Sean D ^b   Prevelige Jr , Peter E ^b   Foguel, Debora ^a  

^a FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

^b University of Alabama at Birmingham   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

REFOLDING PROCESSES; SPECTROSCOPIC TECHNIQUES; UNFOLDING PATHWAY;

BACTERIOPHAGES; DENATURATION; DNA; HYDROSTATIC PRESSURE; MONOMERS; SIZE EXCLUSION CHROMATOGRAPHY; SPECTROSCOPIC ANALYSIS;

PROTEINS;

DNA; MICROORGANISM PROTEIN; MONOMER; POLYMER; PORTAL PROTEIN; UNCLASSIFIED DRUG; UREA;

ARTICLE; BACTERIOPHAGE P22; ELECTRON MICROSCOPY; GEL PERMEATION CHROMATOGRAPHY; HYDROSTATIC PRESSURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROSCOPY;

BACTERIOPHAGE P22; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; DOSE-RESPONSE RELATIONSHIP, DRUG; HYDROSTATIC PRESSURE; LIGHT; MODELS, CHEMICAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RENATURATION; PROTEIN STRUCTURE, TERTIARY; SCATTERING, RADIATION; TEMPERATURE; UREA; VIRAL PROTEINS;

EID: 34250862659     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700006d     Document Type: Article

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