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. 2009 Mar 19;10(3):1314–1345. doi: 10.3390/ijms10031314

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© 2009 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Figure 3. — Kinetics of thermal aggregation of GAPDH (0.4 mg/mL) at 55 °C. The dependences of the hydrodynamic radius of the protein aggregates (R_h) on time obtained at various concentrations of the enzyme: (1) 0.05, (2) 0.2, (3) 0.3 and (4) 0.4 mg/mL. (A) Full kinetic curves. The solid curves are calculated from Equation (8). (B) The initial parts of the dependences of R_h on time. The solid lines were calculated from Equation (9). The horizontal dotted line corresponds to the R_h,0 value (R_h,0 = 22 nm).