  We present a microscopic variational theory for the free energy surface of a
fast folding protein that allows folding kinetics to be resolved to the residue
level using Debye-Waller factors as local order parameters. We apply the method
to lambda-repressor and compare with site directed mutagenesis experiments. The
formation of native structure and the free energy profile along the folding
route are shown to be well described by the capillarity approximation but with
some fine structure due to local folding topology.
