Residual structures in the unfolded state of starch-binding domain of glucoamylase revealed by near-UV circular dichroism and protein engineering techniques.

Abstract

Protein folding is a thermodynamic process driven by energy gaps between the native and unfolded states. Although a wealth of information is available on the structure of folded species, there is a paucity of data on unfolded species. Here, we analyzed the structural properties of the unfolded state of the starch-binding domain of glucoamylase from… (More)
DOI: 10.1016/j.bbapap.2016.05.002

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Cite this paper

@article{Ota2016ResidualSI, title={Residual structures in the unfolded state of starch-binding domain of glucoamylase revealed by near-UV circular dichroism and protein engineering techniques.}, author={Chiaki Ota and Masamichi Ikeguchi and Akiyoshi Tanaka and Daizo Hamada}, journal={Biochimica et biophysica acta}, year={2016}, volume={1864 10}, pages={1464-72} }