The study of protein folding is both a theoretical and an experimental discipline. But whereas experimentalists generally study specific proteins, theoreticians often use models that apply only to generic proteins. Can the two be reconciled? One study goes some way towards this through a statistical analysis of measured folding rates and theoretical determinants. The authors conclude that, for one group of proteins, the speed of folding depends on the number of local versus non-local contacts between amino-acid residues in the protein.
