Inhibition of amyloid fibril formation of hen egg white lysozyme by trimethylamine N-oxide at low pH

International Journal of Biological Macromolecules

Volumn 70, Issue , 2014, Pages 214-221

  Wawer, Jarosław ^a   Krakowiak, Joanna ^a   Szociński, Michał ^a   Lustig, Zofia ^a   Olszewski, Marcin ^a   Szostak, Kamila ^a  

^a GDANSK UNIVERSITY OF TECHNOLOGY   (Poland)

Author keywords

Amyloid inhibition; Hen egg white lysozyme; Protein aggregation; Protein dimerisation; Trimethylamine N oxide

Indexed keywords

AMYLOID; HEN EGG WHITE LYSOZYME; LYSOZYME; TRIMETHYLAMINE OXIDE; UNCLASSIFIED DRUG; EGG WHITE; HEN EGG LYSOZYME; METHYLAMINE; TRIMETHYLOXAMINE;

ACIDITY; ARTICLE; ATOMIC FORCE MICROSCOPY; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; COVALENT BOND; DENSITOMETRY; GEL ELECTROPHORESIS; IN VITRO STUDY; LIGHT SCATTERING; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN FIBRILLATION; PROTEIN PROCESSING; PROTEIN STABILITY; PROTEIN SYNTHESIS INHIBITION; PROTEIN UNFOLDING; PROTON TRANSPORT; STRUCTURE ANALYSIS; ULTRAVIOLET SPECTROSCOPY; ANIMAL; CHEMISTRY; FEMALE; PH; ULTRASTRUCTURE;

AMYLOID; ANIMALS; EGG WHITE; FEMALE; HYDROGEN-ION CONCENTRATION; METHYLAMINES; MURAMIDASE;

EID: 84904470984     PISSN: 01418130     EISSN: 18790003     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2014.06.057     Document Type: Article

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