---
_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'
...