The adsorption of the amino acid L-cysteine (L-Cys) onto the Ag(110) surface at room temperature is investigated using reflection anisotropy spectroscopy (RAS). The adsorption of L-Cys at metal surfaces offers a route to the immobilisation of proteins with potential applications in the nanoscale fabrication of biomaterial surfaces. L-Cys binds strongly to Ag(110) by the formation of a thiolate linkage. Heating the L-Cys saturated surface to 580 K results in the decomposition of the adsorbate, leaving a chemisorbed S adlayer with a c(8 × 2) structure.1 Introduction The self-assembly of organic molecules into thin films at material surfaces is a process that offers a flexible route to the nanoscale engineering of chemically functionalised surfaces with applications in molecular electronics, corrosion inhibition, sensors and biomaterials. The surface-sensitive linear optical technique of reflection anisotropy spectroscopy (RAS) [1][2][3], in combination with electron-based probes, has been used to monitor the growth of ultra-high vacuum (UHV) deposited molecular films and RAS has shown sensitivity to molecular orientation and assembly [4][5][6][7]. These previous RAS studies have focused on the Cu(110) substrate to induce ordered anisotropy in the growing film and have exploited molecular adsorbates that interact via the Cu-carboxylate interaction.Another molecule-substrate interaction of technological importance is the metal-thiolate bond. This interaction is exploited in the routine preparation of self assembled monolayers of alkane-thiol molecules at Au surfaces [8,9]. While the Au-thiol interaction has been well studied, relatively little is currently known about the self-assembly and bonding of thiols on other metal surfaces.In the work presented here, we investigate the adsorption of the amino acid L-cysteine (L-Cys) [HS-CH 2 -CH(NH 2 )-COOH] on Ag(110). L-Cys contains a thiol (-SH) group and is known to adsorb onto Au surfaces via a thiolate (Au-S) linkage [10]. The adsorption of L-Cys at metal surfaces offers a route to the immobilisation of proteins with potential applications in the nanoscale fabrication of biomaterial surfaces. We find evidence for L-Cys binding to the Ag(110) surface through an Ag-thiolate linkage. Heating the L-Cys saturated surface results in the decomposition of the adsorbed L-Cys and leaves behind an ordered S adlayer.