  In this paper we discuss a one-dimensional Abelian Higgs model with
Chern-Simons interaction as an effective theory of one-dimensional curves
embedded in three-dimensional space. We demonstrate how this effective model is
compatible with the geometry of protein molecules. Using standard field theory
techniques we analyze phenomenologically interesting static configurations of
the model and discuss their stability. This simple model predicts some
characteristic relations for the geometry of secondary structure motifs of
proteins, and we show how this is consistent with the experimental data. After
using the data to universally fix basic local geometric parameters, such as the
curvature and torsion of the helical motifs, we are left with a single free
parameter. We explain how this parameter controls the abundance and shape of
the principal motifs (alpha helices, beta strands and loops connecting them).
