Spatial extent of charge repulsion regulates assembly pathways for lysozyme amyloid fibrils

PLoS ONE

Volumn 6, Issue 4, 2011, Pages

  Hill, Shannon E ^a   Miti, Tatiana ^a   Richmond, Tyson ^a   Muschol, Martin ^a  

^a UNIVERSITY OF SOUTH FLORIDA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; EGG WHITE; LYSOZYME; MONOMER; OLIGOMER; HEN EGG LYSOZYME; SODIUM CHLORIDE;

ARTICLE; CONTROLLED STUDY; ENTROPY; HEN; IONIC STRENGTH; MOLECULAR INTERACTION; NONHUMAN; PRECIPITATION; PROTEIN ASSEMBLY; PROTEIN DENATURATION; ANIMAL; CHEMISTRY; DOSE RESPONSE; DRUG EFFECT; ENZYME STABILITY; HUMAN; KINETICS; LIGHT; METABOLISM; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; RADIATION SCATTERING; TEMPERATURE;

AMYLOID; ANIMALS; CHEMICAL PRECIPITATION; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME STABILITY; HUMANS; KINETICS; LIGHT; MURAMIDASE; PROTEIN DENATURATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; SCATTERING, RADIATION; SODIUM CHLORIDE; TEMPERATURE;

EID: 79953695682     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0018171     Document Type: Article

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