Immobilisation of proteins by atomic clusters on surfaces
Related Experiment Video
Updated: Jul 18, 2026

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
Published on: August 20, 2018
1Nanoscale Physics Research Laboratory, School of Physics and Astronomy, The University of Birmingham, Edgbaston, Birmingham B15 2TT, UK. r.e.palmer@bham.ac.uk
Abstract:
In this Opinion article, we describe a nanotechnology-based approach to immobilize and orient proteins onto surfaces using atomic clusters prepared by physical methods. This is relevant to future protein biochips where dilute arrays of protein binding sites, each designed to immobilize no more than one protein molecule, would be ideal. In the case of a surface consisting of size-selected atomic gold clusters, proteins containing free cysteine residues can chemisorb directly to the bare cluster surface, thus effecting oriented immobilisation. The selection of atomic gold clusters in the size range 1-100 atoms (<3nm in diameter) is intended to ensure that, typically, only one protein can bind directly to the cluster surface. These nanoclusters of a smaller size scale than that of the protein present minimal contact between the gold and the protein, and hence imply a reduced risk of protein denaturing compared with gold films or extended surfaces.
More Related Videos
Related Concept Videos
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein-protein Interfaces
Molecular Chaperones and Protein Folding
The...
Mechanisms of Membrane Domain Formation
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Protein Diffusion in the Membrane

