A little walk from physical to biological complexity: protein folding and stability

Abstract

As an example of topic where biology and physics meet, we present the issue of protein folding and stability, and the development of thermodynamics-based bioinformatics tools that predict the stability and thermal resistance of proteins and the change of these quantities upon amino acid substitutions. These methods are based on knowledge-driven statistical potentials, derived from experimental protein structures using the inverse Boltzmann law. We also describe an application of these predictors, which contributed to the understanding of the mechanisms of aggregation of a particular protein known to cause a neuronal disease.\n\n\n\nO_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=150 SRC=\"FIGDIR/small/043737_ufig1.gif\" ALT=\"Figure 1000\">\nView larger version (98K):\norg.highwire.dtl.DTLVardef@1fb262borg.highwire.dtl.DTLVardef@186eaaforg.highwire.dtl.DTLVardef@99b828org.highwire.dtl.DTLVardef@953a2_HPS_FORMAT_FIGEXP M_FIG C_FIG