Reversible folding of cysteine-rich metallothionein by an overcritical reaction path Export

@article{citeulike:2858984, abstract = {A first-order-like state transition is considered to be involved in the restoration of the activities of a few proteins by correctly folding the protein [Phys. Rev. E 66 (2002) 021903]. In order to understand the general applicability of this mechanism, we studied a metallothionein (MT) protein with an unconventional structure, i.e., without any [alpha]-helix or [beta]-sheet. MT is a 61 amino-acid peptide. There are 6-7 Zn2+ ions, which bind avidly to 20 conserved cysteines (Cys) of MT. These properties indicate that the structure of MT is quite different from those of the other proteins. Similar to our previous findings, the denatured MT can be folded without any aggregation via a designated stepwise quasi-static process (an over-critical reaction path). The particle size of folded MT intermediates, determined by dynamic light scattering, shrank right after the first folding stage. It is consistent with a collapse-model. In addition, results from both atomic absorption and circular dichroism (CD) indicate that the stable intermediates may fold to the native conformation but with only partial Zn2+ binding, which in turn implies that those folding intermediates are in a molten globular state. These reversible unfolding and folding processes indicate that Cys-rich protein, MT, may also be folded by way of a first-order-like state transition mechanism. We suspect that this process may likely be involved in the reaction of the metal substitution process in metal containing enzymes.}, author = {Liu, Yi-Liang and Lee, Hui-Ting and Chang, Chia-Ching and Kan, Lou-Sing}, citeulike-article-id = {2858984}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/S0006-291X(03)00899-4}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6WBK-48M7TX3-P/1/8203a2742394f78d559fbbc650b1551b}, day = {20}, doi = {10.1016/S0006-291X(03)00899-4}, journal = {Biochemical and Biophysical Research Communications}, keywords = {folding, metallothionein}, month = {June}, number = {1}, pages = {59--63}, posted-at = {2008-06-03 13:17:58}, priority = {3}, title = {Reversible folding of cysteine-rich metallothionein by an overcritical reaction path}, url = {http://dx.doi.org/10.1016/S0006-291X(03)00899-4}, volume = {306}, year = {2003} }

TY - JOUR ID - citeulike:2858984 L3 - citeulike-article-id:2858984 N2 - A first-order-like state transition is considered to be involved in the restoration of the activities of a few proteins by correctly folding the protein [Phys. Rev. E 66 (2002) 021903]. In order to understand the general applicability of this mechanism, we studied a metallothionein (MT) protein with an unconventional structure, i.e., without any [alpha]-helix or [beta]-sheet. MT is a 61 amino-acid peptide. There are 6-7 Zn2+ ions, which bind avidly to 20 conserved cysteines (Cys) of MT. These properties indicate that the structure of MT is quite different from those of the other proteins. Similar to our previous findings, the denatured MT can be folded without any aggregation via a designated stepwise quasi-static process (an over-critical reaction path). The particle size of folded MT intermediates, determined by dynamic light scattering, shrank right after the first folding stage. It is consistent with a collapse-model. In addition, results from both atomic absorption and circular dichroism (CD) indicate that the stable intermediates may fold to the native conformation but with only partial Zn2+ binding, which in turn implies that those folding intermediates are in a molten globular state. These reversible unfolding and folding processes indicate that Cys-rich protein, MT, may also be folded by way of a first-order-like state transition mechanism. We suspect that this process may likely be involved in the reaction of the metal substitution process in metal containing enzymes. IS - 1 JF - Biochemical and Biophysical Research Communications EP - 63 TI - Reversible folding of cysteine-rich metallothionein by an overcritical reaction path VL - 306 SP - 59 KW - folding KW - metallothionein AU - Liu, Yi-Liang AU - Lee, Hui-Ting AU - Chang, Chia-Ching AU - Kan, Lou-Sing PY - 2003/06/20/ UR - http://dx.doi.org/10.1016/S0006-291X(03)00899-4 ER -