Absence of the thermal transition in apo-alpha-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry.
To estimate the energy level of the molten globule state, the heat capacity function of apo-alpha-lactalbumin in the molten globule state has been examined using a scanning microcalorimeter at neutral pH. The results showed that the enthalpy difference between the molten globule state and presumed unfolded state by heating was almost zero at neutral pH, demonstrating that the molten globule state does not exhibit any co-operative transition upon heating. This is in agreement with the results already reported at acid pH, but is apparently in conflict with that recently reported with some assumptions at neutral pH.
Yutani
K
K
Institute for Protein Research, Osaka University, Japan.
Ogasahara
K
K
Kuwajima
K
K
D001059:Apoproteins / Q000737:chemistry*; D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D007768:Lactalbumin / Q000737:chemistry*; D017510:Protein Folding; D013816:Thermodynamics
D001059:Apoproteins; C041966:apo-alpha-lactalbumin; D007768:Lactalbumin