Proteins display a tremendous range of specific biological function.  Applying this function to sensing, chemical catalysis, and biofuel generation would profoundly expand and change these traditional fields.  This goal requires that the protein of interest be effectively integrated with inorganic materials such as a crystal surface in a controlled and oriented manner without altering its three-dimensional fold or compromising function, a challenging biomaterials problem. In the research described here, we chemically functionalize gold surfaces with peptides of known secondary structure.  These surfaces are chemically characterized through X-ray photoelectron spectroscopy, ellipsometry, and surface infrared spectroscopy.  Furthermore, we use surface infrared and circular dichroic spectroscopies to characterize the structure and orientation of the peptide on the surface.  We demonstrate that correctly functionalized surfaces induce a alpha-helical secondary structure on a peptide that is disordered in solution. Demonstration of the control over a desired secondary structure of helical elements at a chemically functionalized surface is an important advance in preparing robust biologically mimetic surfaces and is expected to lead to an entirely new mechanism through which biological and inorganic materials can be coaxed to interact.