Structural determinants of the rate of protein folding

To understand the mechanism of protein folding and to assist rational design of fast-folding, non-aggregating and stable artificial enzymes, it is essential to determine the structural parameters which govern the rate constants of folding, k f . It has been found that −log k f is a linear function of the so-called chain topology parameter ( CTP) within the range of 10 −1 s −1⩽ k f ⩽10 8 s −1. The correlation between −log k f and CTP is much improved than using previously published contact order ( CO) method. It has been further suggested that short sequence separations may be preferred for the establishment of stable interactions for the design of novel artificial enzymes and the modification of slow-folding proteins with aggregating intermediates.