Thermodynamics of protein self-association and unfolding. The case of apolipoprotein A-I.
about
Identification of an amyloid fibril forming peptide comprising residues 46-59 of apolipoprotein A-ISecondary structure changes in ApoA-I Milano (R173C) are not accompanied by a decrease in protein stability or solubility.Thermal protein unfolding by differential scanning calorimetry and circular dichroism spectroscopy Two-state model versus sequential unfolding.
P2860
Thermodynamics of protein self-association and unfolding. The case of apolipoprotein A-I.
description
2012 nî lūn-bûn
@nan
2012 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2012年の論文
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2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
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2012年论文
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name
Thermodynamics of protein self-association and unfolding. The case of apolipoprotein A-I.
@ast
Thermodynamics of protein self-association and unfolding. The case of apolipoprotein A-I.
@en
type
label
Thermodynamics of protein self-association and unfolding. The case of apolipoprotein A-I.
@ast
Thermodynamics of protein self-association and unfolding. The case of apolipoprotein A-I.
@en
prefLabel
Thermodynamics of protein self-association and unfolding. The case of apolipoprotein A-I.
@ast
Thermodynamics of protein self-association and unfolding. The case of apolipoprotein A-I.
@en
P2093
P356
P1433
P1476
Thermodynamics of protein self-association and unfolding. The case of apolipoprotein A-I.
@en
P2093
F Zehender
H-J Schönfeld
P304
P356
10.1021/BI2013799
P407
P577
2012-02-03T00:00:00Z