Effect of non-native helix destabilization on the folding of equine {beta}-lactoglobulin

β-lactoglobulin forms a non-native α-helix during an early stage of folding. To address the role of the non-native structure in the folding process, we designed several mutants of equine β-lactoglobulin with reduced helical propensity in the non-native helix region. One of them, A123T, showed a similar structure to that of the wild-type protein; its folding kinetics was investigated by stopped-flow circular dichroism (CD) and fluorescence. Although A123T showed a reduced burst-phase CD intensity, its folding rate was similar to that of the wild-type protein, which indicated that the formation of the non-native helix does not accelerate or decelerate the folding reaction.

Source: Journal of Biochemistry - October 27, 2014 Category: Biochemistry Authors: Okabe, T., Miyajima, T., Nakagawa, K., Tsukamoto, S., Fujiwara, K., Ikeguchi, M. Tags: Regular Papers Source Type: research