Effect of hydrostatic pressure on unfolding of α-lactalbumin: Volumetric equivalence of the molten globule and unfolded state

The effect of pressure on the unfolding of bovine α-lactalbumin was investigated by ultraviolet absorption methods. The change of molar volume associated with unfolding, ΔV, was measured in the presence or absence of guanidine hydrochloride at pH 7. The ΔV was estimated to be −63 cm3/mol in the abse...

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Veröffentlicht in:	Protein science 1999-12, Vol.8 (12), p.2765-2772
Hauptverfasser:	KOBASHIGAWA, YOSHIHIRO, SAKURAI, MASAO, NITTA, KATSUTOSHI
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Cattle Circular Dichroism folding Guanidine hydration Hydrostatic Pressure Lactalbumin - chemistry molten globule Protein Conformation Protein Folding volume change α‐lactalbumin
Online-Zugang:	Volltext
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