Abstract

When amino acid residues are represented by parameters describing their side chain lengths and polarities, a sequence function defined as the sum of the first two sequence autocorrelation functions is found to be negatively and linearly correlated with the logarithms of folding rates of β-proteins. The new function reveals new features in β-protein folding: larger residues slow down the folding while alternative distribution of polar-non-polar residues accelerates the folding.

Keywords: Protein, polar-non-polar residues