The role that alkyl chain packing density in a self-assembled monolayer (SAM) plays in the adsorption of protein to the SAM surface was investigated using in situ neutron reflectivity (NR) and total internal reflection fluorescence (TIRF) measurements of the adsorption behavior of human serum albumin (HSA) and human immunoglobulin G (HGG). The proteins differ particularly in the fact that HSA has specific binding pockets for alkyl chains while HGG does not. NR results show that HSA adsorbs from a 1.0 mg/mL solution as a single layer on the SAMs, with the protein interpenetrating into a less densely packed SAM, but not into a more densely packed SAM. Likewise, the kinetics of the HSA adsorption to the SAMs varies markedly with the alkyl chain packing. In contrast, both the structure of the adsorbed layer and adsorption kinetics vary little with the alkyl chain packing density in the case of HGG adsorbing from solution. HGG also does not penetrate into loosely packed SAMs. NR results reveal that the HGG adsorbs as two layers, with the layer closest to the SAM being more tightly packed. When HSA and HGG compete for adsorption sites on a SAM, HGG effectively displaces HSA from a tightly packed SAM, but does not compete effectively with HSA adsorbed tenaciously onto a loosely packed SAM.