Figure 3 : Structure of the cross-[beta] spine of amyloid-like fibrils : Nature

From the following article:

Structure of the cross- beta spine of amyloid-like fibrils

Rebecca Nelson, Michael R. Sawaya, Melinda Balbirnie, Anders Ø. Madsen, Christian Riekel, Robert Grothe and David Eisenberg

Nature 435, 773-778(9 June 2005)

doi:10.1038/nature03680

BACK TO ARTICLE

The standard free energy change Delta G⁰ for the conversion is small, so that the change in Delta G is controlled mainly by the concentration of monomer. At low concentrations, the monomeric state is favoured over the aggregated state, and the aggregated state is favoured at high concentrations. There is a significant kinetic barrier to formation of the aggregated state, Delta G^‡_formation. At high concentrations of protein, the barrier to re-dissolve fibres, Delta G^‡_dissolution, is very large.

Previous figureFigures & Tables index

BACK TO ARTICLE

FIGURE 3. A conjectural plot of the free energy, G, for conversion of monomeric GNNQQNY, M, to the aggregated state, Mn.

From the following article:

FIGURE 3. A conjectural plot of the free energy, G, for conversion of monomeric GNNQQNY, M, to the aggregated state, M_n.