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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Popis
Shrnutí:	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 equilibrium of disulfide‐deficient variant of hen lysozyme amyloid protofibril. Based on the density profiles, the partial molar volume and thermal expansibility changes for dissociation, ΔvD and ΔeD, were obtained to be −74 cm3/mol at 25°C and −2.3 cm3 mol−1 K−1, respectively. The dissociation of amyloid fibril destroys the cross β‐structure, and such conformational destruction in native protein fold rarely accompanies negative thermal expansibility change. We discussed the negative thermal expansibility change in terms of hydration and structural packing of the amyloid protofibril.
Bibliografie:	istex:75958BEBF56149E934492E0F73BD96AA308E79B7 ark:/67375/WNG-4FRPD6JM-1 ArticleID:ELPS5395 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0173-0835 1522-2683 1522-2683
DOI:	10.1002/elps.201400468