Though chlorophyll-binding protein CP29, a light harvesting complex in photosystem II of green plants, is proposed to play a role in the regulation of potentially-damaging excess chlorophyll excitations in the supercomplex, little is known about its spatial structure and its relation to excitation energy transfer dynamics and photoprotective action. In vivo, the presence of carotenoid pigment zeaxanthin is correlated with the quenching of excess chlorophyll excitations. Although the mechanism of quenching is still unknown, it is evident that CP29 exchanges carotenoid pigments depending on illumination conditions--in low light, the complex binds violaxanthin, while in high light zeaxanthin is bound.We probe the chlorophyll Qy band of isolated CP29, binding either violaxanthin or zeaxanthin, using conventional and polarization-sensitive two-dimensional electronic spectroscopy (2DES) in order to better characterize electronic and spatial structure. 2DES resolves both excitation and emission energy of the molecular complexes being studied, providing a picture of the correlations between multiple excited states and revealing the presence of states that may go undetected by other spectroscopies. It also provides a direct map of excitation energy transfer processes within the complex by identifying signals from correlated donor and acceptor energies. Polarization-dependent studies provide clues in particular about chromophore configuration. We furthermore investigate whether the binding of zeaxanthin alters the excitation energy landscape and the resulting dynamics of CP29 to potentially modulate the quenching of excess excitations.(Supported by the Office of Basic Energy Sciences, Chemical Sciences Division, U.S. Department of Energy (contract DE-AC03-76S98) and a Seaborg Fellowship to NSG from LBNL).