Many organisms use macromolecules, often proteins or peptides, to control,, the growth of inorganic crystals into complex materials. The ability to model peptide-mineral interactions accurately could allow for the design of navel peptides to produce materials with desired properties. Here; We tested a computational devloped to prdict the structure of peptides on mineral Surfaces. Using this algorithm, We analyzed energetic and structural differences between a 16 residue peptide, (bap4) designed to interact with a, calcite growth plane and single- and double-point Mutations of the charged residues Currently, no experimental method is available to resolve the structures of Proteins on solid surfaces, which precludes benchrnarking for computational models. Therefore, to test the models, we chemically synthesized each peptide and analyzed its effects on calcite crystal growth. Whereas bap4 affected the crystal growth by producing heavily stepperd corners and edges, point mutants had variable influences on morphology. Calculated residue-specific binding energies correlated with experimental observations; point mutations of residues predicted to be crucial to surface interactions produced morphologies most similar to unmodified calcite. These results suggest that peptide conformation plays a role in mineral interactions and that the computational model supplies valid energetic and structural data that can provide information about expectecl,crystal morphology.