Optical tweezers have been characterized and used to investigate biomolecular bonds. The optical trap can be approximated by a harmonic potential well, and two methods to determine the force constant associated with this harmonic potential are discussed. The dependence of the force constant on laser power and on the distance from the cover glass has been determined, and is in qualitative agreement with theory and literature. It has been shown that biomolecular bonds of the model system protein G-IgG can be ruptured using optical tweezers. Bond rupture is statistical of nature, and most probable single bond rupture forces were determined to be 4310 pN at a loading rate of 450 pN/s and 6014 pN at a loading rate of 950 pN/s. This is in agreement with values reported in literature on similar systems.