Abstract: We present a simple physical model which demonstrates that the native state folds of proteins can emerge on the basis of considerations of geometry and symmetry.  We show that the inherent anisotropy of a chain molecule, the geometrical and energetic constraints placed by the hydrogen bonds and sterics, and hydrophobicity are sufficient to yield a free energy landscape with broad minima even for a homopolymer.  These minima correspond to marginally compact structures comprising the menu of folds that proteins choose from to house their native-states in.  Our results provide a general framework for understanding the common characteristics of globular proteins.