Sampling Protein Form and Function with the Atomic Force MicroscopeBaclayon, M., Roos, W. H. & Wuite, G. J. L., Aug-2010, In : Molecular & Cellular Proteomics. 9, 8, p. 1678-1688 11 p.
Research output: Contribution to journal › Review article › Academic › peer-review
To study the structure, function, and interactions of proteins, a plethora of techniques is available. Many techniques sample such parameters in non-physiological environments (e. g. in air, ice, or vacuum). Atomic force microscopy (AFM), however, is a powerful biophysical technique that can probe these parameters under physiological buffer conditions. With the atomic force microscope operating under such conditions, it is possible to obtain images of biological structures without requiring labeling and to follow dynamic processes in real time. Furthermore, by operating in force spectroscopy mode, it can probe intramolecular interactions and binding strengths. In structural biology, it has proven its ability to image proteins and protein conformational changes at submolecular resolution, and in proteomics, it is developing as a tool to map surface proteomes and to study protein function by force spectroscopy methods. The power of AFM to combine studies of protein form and protein function enables bridging various research fields to come to a comprehensive, molecular level picture of biological processes. We review the use of AFM imaging and force spectroscopy techniques and discuss the major advances of these experiments in further understanding form and function of proteins at the nanoscale in physiologically relevant environments. Molecular & Cellular Proteomics 9:1678-1688, 2010.
|Number of pages||11|
|Journal||Molecular & Cellular Proteomics|
|Publication status||Published - Aug-2010|
- MOLECULAR-DYNAMICS SIMULATION, TITIN IMMUNOGLOBULIN DOMAINS, COLI RNA-POLYMERASE, SINGLE-MOLECULE, MECHANICAL-PROPERTIES, HIGH-RESOLUTION, VIRAL CAPSIDS, MEMBRANE-PROTEINS, VIRUS CAPSIDS, LIVING CELLS