An early intermediate of refolding α‐lactalbumin forms within 20 ms

Abstract
The kinetics of α-lactalbumin refolding were studied by the stopped-flow method with the registration of CD and intrinsic fluorescence at several wavelengths. It was shown that the early kinetic intermediate forms during the dead-time of the experiment (20 ms). This intermediate has a considerable amount of secondary structure and unpolar clusters in its molecular structure but has no rigid tertiary structure.