The adsorption of proteins from solution onto solid surfaces has attracted much attention due to its scientific importance and application in many areas. In the medical and food processing industries, for example, it is usually required to remove adsorbed proteins since even a small amount of deposited protein gives rise to subsequent adsorption of fibrous proteins, leading to adverse biological consequences. On the other hand, controlled immobilization of proteins is crucial in the field of biotechnology where well-ordered protein layers may lead to a new generation of reactor beds for catalysis, biosensors, and disease diagnostics. Previous studies have shown that protein adsorption is intimately related to surface properties such as hydrophobicity and surface charge density. In this experiment, adsorption of lysozyme on modified gold surfaces was studied by Fourier transform infrared spectroscopy (FTIR). Surface modification was conducted by two ways, formation of alkanethiolate self-assembled monolayers (SAMs) and spin-cast of polymers on the gold surface. Three SAMs with different end groups (hydrophobic and neutral methyl group (CH3), hydrophilic and neutral hydroxyl group (OH), and hydrophilic and negatively charged carboxyl group (COOH)) were prepared using corresponding thiols in ethanol. Thin films of hydrophobic polystyrene, poly(methylmethacrylate), and poly(benzylmethacrylate) and hydrophilic poly(2-hydroxyethyl methacrylate) were deposited on the gold surface by spin-casting polymer solution. FTIR data by specular reflection mode and surface hydrophobicity before and after lysozyme adsorption will be presented and discussed.