Jump to main content
Jump to site search

Issue 5, 2002
Previous Article Next Article

The scanning probe microscopy of metalloproteins and metalloenzymes

Author affiliations

Abstract

In recent years, the concept of microscopy and the ability to study processes at a truly molecular level have been revolutionised by the development of a family of instruments based on acquiring data through the scanning of a proximal probe across a surface. Scanning Probe Microscopes (SPMs) enable surface-confined structures to be resolved at ångstrom-resolution, in real time, and under a variety of controllable conditions. Despite initial difficulties, much progress has been in the application of this technology to the high-resolution analysis of biological systems; these have varied from complex cellular systems to molecular biopolymers. Studying the interactions of protein with surfaces has been intrinsic to the development of our understanding of blood coagulation, fibrinolysis, thrombus formation and the synthesis of biocompatible materials. The specific interactions of metalloproteins and enzymes with electrode surfaces remains central to the understanding of the bioelectrochemical processes and to the development of biosensing devices. Though ellipsometry, Raman, microcalorimetry, surface plasmon resonance, and other spectroscopic methods, can provide much information on these interfaces, the acquired data are averaged over a large number of molecular species with a low spatial resolution. Proximal probe methods have much to offer in this regard and have revolutionized our ability to monitor such interactions.

Graphical abstract: The scanning probe microscopy of metalloproteins and metalloenzymes

Back to tab navigation

Publication details

The article was received on 07 Sep 2001, accepted on 23 Nov 2001 and first published on 01 Feb 2002


Article type: Feature Article
DOI: 10.1039/B108128B
Citation: Chem. Commun., 2002,0, 393-401
  •   Request permissions

    The scanning probe microscopy of metalloproteins and metalloenzymes

    J. J. Davis and H. A. O. Hill, Chem. Commun., 2002, 0, 393
    DOI: 10.1039/B108128B

Search articles by author

Spotlight

Advertisements