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Is the molten globule a third thermodynamic state of protein? The example of α-lactalbumin

✍ Scribed by Wolfgang Pfeil

Publisher: John Wiley and Sons
Year: 1998
Tongue: English
Weight: 91 KB
Volume: 30
Category: Article
ISSN: 0887-3585
DOI: 10.1002/(sici)1097-0134(19980101)30:1<43::aid-prot4>3.0.co;2-l

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✦ Synopsis

Thermal and denaturant-induced transitions of the acid molten globule state of bovine ␣-lactalbumin (acid [A] state) are analyzed by scanning calorimetry, titration calorimetry, viscosimetry, and derivative spectroscopy. A denaturant-induced heat effect of the A state is shown by a calorimetric difference titration of the A-state versus unfolded (reduced) ␣-lactalbumin. However, changes of viscosity and derivative spectra do not parallel the heat effect. At thermal denaturation monitored by derivative spectroscopy and scanning microcalorimetry the presence of a gradual transition in ␣-lactalbumin A state is shown. The results are consistent with the existence of tertiary interactions in the A state and the absence of a cooperative unfolding transition of the molten globule. The results do not support the idea that the molten globule is a third thermodynamic state.

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