The adsorption of protein films onto solid surfaces, both artificial and naturally occurring, has been widely studied using a variety of techniques due to its importance in medicine, biomedical applications, and the general understanding of protein structure and function. We have begun a project that uses the technique of in situ x-ray reflectivity to obtain highly resolved structural information with time resolution on the order of minutes. This talk will present the results of our studies of protein films of serum albumin, immunoglobulin G, and lysozyme on hydrophobic self-assembled monolayers and on bare, hydrophilic silicon oxide. The protein films are readily observable, showing extensive denaturing after adsorption with a slow decay of density into the aqueous solution. Comparisons to films that are removed from solution, the influence of solution concentration, the effects of x-ray damage, and the time scales for protein film formation and evolution will also be discussed.