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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Published in:Electrophoresis Vol. 36; no. 6; pp. 893 - 901
Main Authors: Ishiguro, Ryo, Matsuo, Hiroshi, Kameyama, Keiichi, Tachibana, Hideki, Fujisawa, Tetsuro
Format: Journal Article
Language:English
Published: Germany Blackwell Publishing Ltd 01.03.2015
Subjects:
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
Online Access:Get full text
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Summary: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.
Bibliography: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