COVALENT ANCHORING OF PROTEINS ONTO GOLD-DIRECTED NHS-TERMINATED SELF-ASSEMBLED MONOLAYERS IN AQUEOUS BUFFERS - SFM IMAGES OF CLATHRIN CAGES AND TRISKELIA

N-hydroxysuccinimide-terminated self-assembled monolayers with linear (CH2)(10) chains were prepared on ultraflat Au(111) surfaces from dith iobis(succinimidylundecanoate). These monolayers, which are covalently chemisorbed to gold via thiolate bonds, form a highly reactive amino- group specific carpet at the liquid-solid interface. Proteins bind to it covalently in aqueous buffers under mild conditions; this provides a (general) procedure for protein immobilization for scanning probe mi croscopy. Using this technique, we have obtained what we believe are t he first scanning force microscopy images of clathrin cages and of the ir in situ disassembly, yielding typical triskelia under non-denaturin g conditions.