--- _id: '3421' abstract: - lang: eng text: Single molecule experiments provide insight into the individuality of biological macromolecules, their unique function, reaction pathways, trajectories and molecular interactions. The exceptional signal-to-noise ratio of the atomic force microscope allows individual proteins to be imaged under physiologically relevant conditions at a lateral resolution of 0.5–1 nm and a vertical resolution of 0.1–0.2 nm. Recently, it has become possible to observe single molecule events using this technique. This capability is reviewed on various water-soluble and membrane proteins. Examples of the observation of function, variability, and assembly of single proteins are discussed. Statistical analysis is important to extend conclusions derived from single molecule experiments to protein species. Such approaches allow the classification of protein conformations and movements. Recent developments of probe microscopy techniques allow simultaneous measurement of multiple signals on individual macromolecules, and greatly extend the range of experiments possible for probing biological systems at the molecular level. Biologists exploring molecular mechanisms will benefit from a burgeoning of scanning probe microscopes and of their future combination with molecular biological experiments. article_processing_charge: No article_type: review author: - first_name: Daniel full_name: Mueller, Daniel last_name: Mueller - first_name: Harald L full_name: Janovjak, Harald L id: 33BA6C30-F248-11E8-B48F-1D18A9856A87 last_name: Janovjak orcid: 0000-0002-8023-9315 - first_name: Tiina full_name: Lehto, Tiina last_name: Lehto - first_name: Lars full_name: Kuerschner, Lars last_name: Kuerschner - first_name: Kurt full_name: Anderson, Kurt last_name: Anderson citation: ama: Mueller D, Janovjak HL, Lehto T, Kuerschner L, Anderson K. Observing structure, function and assembly of single proteins by AFM. Progress in Biophysics and Molecular Biology. 2002;79(1-3):1-43. doi:10.1016/S0079-6107(02)00009-3 apa: Mueller, D., Janovjak, H. L., Lehto, T., Kuerschner, L., & Anderson, K. (2002). Observing structure, function and assembly of single proteins by AFM. Progress in Biophysics and Molecular Biology. Elsevier. https://doi.org/10.1016/S0079-6107(02)00009-3 chicago: Mueller, Daniel, Harald L Janovjak, Tiina Lehto, Lars Kuerschner, and Kurt Anderson. “Observing Structure, Function and Assembly of Single Proteins by AFM.” Progress in Biophysics and Molecular Biology. Elsevier, 2002. https://doi.org/10.1016/S0079-6107(02)00009-3. ieee: D. Mueller, H. L. Janovjak, T. Lehto, L. Kuerschner, and K. Anderson, “Observing structure, function and assembly of single proteins by AFM,” Progress in Biophysics and Molecular Biology, vol. 79, no. 1–3. Elsevier, pp. 1–43, 2002. ista: Mueller D, Janovjak HL, Lehto T, Kuerschner L, Anderson K. 2002. Observing structure, function and assembly of single proteins by AFM. Progress in Biophysics and Molecular Biology. 79(1–3), 1–43. mla: Mueller, Daniel, et al. “Observing Structure, Function and Assembly of Single Proteins by AFM.” Progress in Biophysics and Molecular Biology, vol. 79, no. 1–3, Elsevier, 2002, pp. 1–43, doi:10.1016/S0079-6107(02)00009-3. short: D. Mueller, H.L. Janovjak, T. Lehto, L. Kuerschner, K. Anderson, Progress in Biophysics and Molecular Biology 79 (2002) 1–43. date_created: 2018-12-11T12:03:14Z date_published: 2002-05-01T00:00:00Z date_updated: 2023-07-17T11:36:32Z day: '01' doi: 10.1016/S0079-6107(02)00009-3 extern: '1' external_id: pmid: - '12225775' intvolume: ' 79' issue: 1-3 language: - iso: eng month: '05' oa_version: None page: 1 - 43 pmid: 1 publication: Progress in Biophysics and Molecular Biology publication_identifier: issn: - 0079-6107 publication_status: published publisher: Elsevier publist_id: '2980' quality_controlled: '1' scopus_import: '1' status: public title: Observing structure, function and assembly of single proteins by AFM type: journal_article user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17 volume: 79 year: '2002' ...