2005
DOI: 10.2174/1389203054546389
|View full text |Cite
|
Sign up to set email alerts
|

Imaging Proteins with Atomic Force Microscopy: An Overview

Abstract: Atomic force microscopy (AFM) has become a common tool for biophysical studies of proteins; mainly due its property to perform characterizations near physiological conditions. The tertiary and quaternary structures, forces driving folding-unfolding processes, and secondary structure elements can be studied in their native environments allowing high resolution level associated with small distortions. This review outlines the operational principles and applications of AFM for protein biophysics.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

1
13
0

Year Published

2006
2006
2020
2020

Publication Types

Select...
5
2
2

Relationship

0
9

Authors

Journals

citations
Cited by 26 publications
(14 citation statements)
references
References 131 publications
(137 reference statements)
1
13
0
Order By: Relevance
“…Since then, AFMs have been adapted with environmental control chambers, and have been retrofitted for microscopy, to investigate biological specimens such as cells. AFMs have been used to examine the mechanics of individual biomolecules [118][119][120], components of the cell nucleus [121,122], cytoskeletal structures [123,124], and whole cells [78,[125][126][127][128][129][130][131][132][133][134][135][136][137][138][139][140]; as well as changes in these mechanics during differentiation [141] and disease progression [142][143][144]. They have also been used to investigate the mechanotransductive response of cells to applied forces [145,146] or ECM stiffness [131,147,148].…”
Section: -4 / Vol 65 November 2013mentioning
confidence: 99%
“…Since then, AFMs have been adapted with environmental control chambers, and have been retrofitted for microscopy, to investigate biological specimens such as cells. AFMs have been used to examine the mechanics of individual biomolecules [118][119][120], components of the cell nucleus [121,122], cytoskeletal structures [123,124], and whole cells [78,[125][126][127][128][129][130][131][132][133][134][135][136][137][138][139][140]; as well as changes in these mechanics during differentiation [141] and disease progression [142][143][144]. They have also been used to investigate the mechanotransductive response of cells to applied forces [145,146] or ECM stiffness [131,147,148].…”
Section: -4 / Vol 65 November 2013mentioning
confidence: 99%
“…AFM alone provides accurate information about the height of a protein, but STM can provide improved lateral information. Tandem STM/AFM has been used to characterize the morphology of metalloproteins such as azurin [15,23,24] .…”
Section: Emerging Techniques For the Study Of Protein Adsorptionmentioning
confidence: 99%
“…AFM images can be obtained in two types of feedback modes: An “AC” mode in which the tip is oscillated at its resonant frequency and a constant amplitude is maintained as the sample is scanned, or in a “DC” (contact) mode in which the tip is brought into direct contact with the surface and the cantilever deflection is kept constant. AFM imaging has been widely used for studying the structure and mechanics of isolated biomolecules [25-27], components of the cell nucleus [28, 29], and subcellular cytoskeletal structures [10, 30]. In addition to imaging, AFM has been successfully used in a force mode in which the tip is held in a fixed horizontal position and used to indent the sample.…”
Section: Tools For Measuring Mechanical Properties Of Single Cellsmentioning
confidence: 99%