extract information about the structural, kinetic, and energetic
properties of the protein molecules from the experimental data of
force-induced protein unfolding measurements. Steered molecular
-dynamics simulations\citep{lu98}, as well as calculations and
-simulations using lattice\citep{lu99} and off-lattice
+dynamics simulations\citep{lu98,lu99}, as well as calculations and
+simulations using lattice\citep{klimov99,socci99} and off-lattice
models\citep{klimov00,li01}, have provided insights into structural
and energetic changes during force-induced protein unfolding.
However, these simulations often involve time scales that are orders
-of magnitude smaller than those of the experiments, and the parameters
-used in the calculations are often neither experimentally controllable
-nor measurable (TODO: example parameters of each type). As a result,
-a Monte Carlo simulation approach based on a simple two-state kinetic
+of magnitude smaller than those of the experiments
+(\cref{sec:single-molecule}), and the parameters used in the
+calculations are often neither experimentally controllable nor
+measurable (TODO: example parameters of each type). As a result, a
+Monte Carlo simulation approach based on a simple two-state kinetic
model for the protein is usually used to analyze data from mechanical
unfolding experiments. A comparison of the force curves measured
experimentally and those generated from simulations can yield the