Hysteresis behavior in the unfolding/refolding processes of a protein trapped in metallo-cages
Takahiro Nakama, Anouk Rossen, Risa Ebihara, Maho Yagi‐Utsumi, Daishi Fujita, Koichi Kato, Sota Sato, Makoto Fujita
Abstract
O media (50 to 90 vol%), the folding structure of a protein sharply denatured at 83 vol%, clearly revealing the regions of initial unfolding. Unfavorable aggregation of the protein leading to irreversible precipitation is completely prevented because of the spatial isolation of the single protein molecule in the cage. When the acetonitrile content reversed (84 to 70 vol%), the once-denatured protein started to regain its original folded structure at 80 vol%, showing that the protein folding/unfolding process can be referred to as a phase transition with hysteresis behavior.
Topics & Concepts
HysteresisChemical physicsCrystallographyBiophysicsMaterials scienceChemistryNanotechnologyPhysicsCondensed matter physicsBiologyProtein Structure and DynamicsEnzyme Structure and FunctionMicrotubule and mitosis dynamics