A variety of experimental and theoretical studies have established that the
folding process of monomeric proteins is strongly influenced by the topology of
the native state. In particular, folding times have been shown to correlate
well with the contact order, a measure of contact locality. Our investigation
focuses on identifying additional topologic properties that correlate with
experimentally measurable quantities, such as folding rates and transition
state placement, for both two- and three-state folders. The validation against
data from forty experiments shows that a particular topologic property which
measures the interdepedence of contacts, termed cliquishness or clustering
coefficient, can account with significant accuracy both for the transition
state placement and especially for folding rates, the linear correlation
coefficient being r=0.71. This result can be further improved to r=0.74, by
optimally combining the distinct topologic information captured by cliquishness
and contact order.Comment: Revtex, 15 pages, 8 figure
