Negative thermal expansibility change for dissociation of lysozyme variant amyloid protofibril

A disulfide‐deficient variant of hen lysozyme, 0SS, is known to form an amyloid protofibril spontaneously, and to dissociate into monomers at high hydrostatic pressure. We carried out native PAGE at various temperatures (20–35°C) and pressures (0.1–200 MPa), to characterize the dissociation equilibr...

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Vydáno v:	Electrophoresis Ročník 36; číslo 6; s. 893 - 901
Hlavní autoři:	Ishiguro, Ryo, Matsuo, Hiroshi, Kameyama, Keiichi, Tachibana, Hideki, Fujisawa, Tetsuro
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	Germany Blackwell Publishing Ltd 01.03.2015
Témata:	amyloid Amyloid - chemistry Amyloid - metabolism Animals Chickens Density Destruction dissociation Dissociation equilibrium Electrophoresis Electrophoresis, Polyacrylamide Gel hens high pressure treatment High-pressure native polyacrylamide gel electro-phoresis Hot Temperature Hydration Hydrostatic pressure Lysozyme Molar volume Monomers Muramidase - chemistry Muramidase - metabolism Partial molar volume polyacrylamide gel electrophoresis Protein Unfolding Proteins temperature Thermal expansibility Thermodynamics Dissociation equilibrium High-pressure native polyacrylamide gel electro-phoresis Thermal expansibility Partial molar volume
ISSN:	0173-0835, 1522-2683, 1522-2683
On-line přístup:	Získat plný text
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