ATOMIC FORCE MICROSCOPE: PROVIDING NEW INSIGHTS ON THE STRUCTURE AND FUNCTION OF LIVING CELLS

1997 ◽  
Vol 21 (11) ◽  
pp. 683-684 ◽  
Author(s):  
B JENA
Keyword(s):  
Atomic Force Microscope ◽  
Living Cells ◽  
Structure And Function ◽  
Atomic Force ◽  
And Function

scholarly journals Single-Cell Elastography: Probing for Disease with the Atomic Force Microscope

2004 ◽  
Vol 19 (2-3) ◽  
pp. 139-154 ◽  
Author(s):  
Kevin D. Costa
Keyword(s):  
Atomic Force Microscope ◽  
Cell Mechanics ◽  
Cell Biology ◽  
Biomechanical Properties ◽  
Living Cells ◽  
Great Promise ◽  
Current Standard ◽  
Atomic Force ◽  
Resolution Imaging ◽  
And Function

The atomic force microscope (AFM) is emerging as a powerful tool in cell biology. Originally developed for high-resolution imaging purposes, the AFM also has unique capabilities as a nano-indenter to probe the dynamic viscoelastic material properties of living cells in culture. In particular, AFM elastography combines imaging and indentation modalities to map the spatial distribution of cell mechanical properties, which in turn reflect the structure and function of the underlying cytoskeleton. Such measurements have contributed to our understanding of cell mechanics and cell biology and appear to be sensitive to the presence of disease in individual cells. This chapter provides a background on the principles and practice of AFM elastography and reviews the literature comparing cell mechanics in normal and diseased states, making a case for the use of such measurements as disease markers. Emphasis is placed on the need for more comprehensive and detailed quantification of cell biomechanical properties beyond the current standard methods of analysis. A number of technical and practical hurdles have yet to be overcome before the method can be of clinical use. However, the future holds great promise for AFM elastography of living cells to provide novel biomechanical markers that will enhance the detection, diagnosis, and treatment of disease.

scholarly journals Unfolding and Folding Proteins

2005 ◽  
Vol 13 (1) ◽  
pp. 3-7
Author(s):  
Stephen W. Carmichael
Keyword(s):  
Molecular Structure ◽  
Atomic Force Microscope ◽  
Structure And Function ◽  
Polyubiquitin Chain ◽  
Small Protein ◽  
Atomic Force ◽  
Single Protein ◽  
Force Clamp ◽  
And Function ◽  
Molecular Structure And Function

The atomic force microscope (AFM) is being utilized in even more clever ways to reveal details of molecular structure and function. As an example, Julio Fernandez and Hongbin Li have used the AFM in the force-clamp mode to monitor the folding trajectory of a single protein. They have demonstrated in a unique way in which a single protein behaves when put under tension, and then what happens when the tension is relieved.Fernandez and Li linked several molecules of ubiquitin, a small protein, together to form a polyubiquitin chain. With one end of the chain attached to a substrate, the tip of a soft cantilever of the AFM attached to a single protein, and from one to nine ubiquitin molecules were picked up.

Structure and Function of Ion Pumps Studied by Atomic Force Microscopy and Gene-transfer Experiments Using Chimeric Na+/K+- and Ca2+ ATPases

1994 ◽  
pp. 264-275
Author(s):  
Kunio Takeyasu ◽  
Jose K. Paul ◽  
Mehdi Ganjeizadeh ◽  
M. Victor Lemas ◽  
Shusheng Wang ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Gene Transfer ◽  
Structure And Function ◽  
Ion Pumps ◽  
Force Microscopy ◽  
Atomic Force ◽  
And Function

Illuminating cellular structure and function in the early secretory pathway by multispectral 3D imaging in living cells

2000 ◽  
Author(s):  
Jens Rietdorf ◽  
David J. Stephens ◽  
Anthony Squire ◽  
Jeremy Simpson ◽  
David T. Shima ◽  
...  
Keyword(s):  
Cellular Structure ◽  
3D Imaging ◽  
Secretory Pathway ◽  
Living Cells ◽  
Structure And Function ◽  
Early Secretory Pathway ◽  
And Function

Expanding the genetic code of mammalian cells

2017 ◽  
Vol 45 (2) ◽  
pp. 555-562 ◽  
Author(s):  
James S. Italia ◽  
Yunan Zheng ◽  
Rachel E. Kelemen ◽  
Sarah B. Erickson ◽  
Partha S. Addy ◽  
...  
Keyword(s):  
Protein Structure ◽  
Amino Acid ◽  
Mammalian Cells ◽  
Living Cells ◽  
Structure And Function ◽  
Unnatural Amino Acid ◽  
Full Potential ◽  
Recent Developments ◽  
Small Footprint ◽  
And Function

In the last two decades, unnatural amino acid (UAA) mutagenesis has emerged as a powerful new method to probe and engineer protein structure and function. This technology enables precise incorporation of a rapidly expanding repertoire of UAAs into predefined sites of a target protein expressed in living cells. Owing to the small footprint of these genetically encoded UAAs and the large variety of enabling functionalities they offer, this technology has tremendous potential for deciphering the delicate and complex biology of the mammalian cells. Over the last few years, exciting progress has been made toward expanding the toolbox of genetically encoded UAAs in mammalian cells, improving the efficiency of their incorporation and developing innovative applications. Here, we provide our perspective on these recent developments and highlight the current challenges that must be overcome to realize the full potential of this technology.

scholarly journals Adhesion forces measured between a calcium blocker drug and its receptor in living cells using atomic force microscope

FEBS Letters ◽  
2003 ◽  
Vol 552 (2-3) ◽  
pp. 155-159 ◽  
Author(s):  
Ricardo de Souza Pereira ◽  
Maria Ivonete Nogueira da Silva ◽  
Mônica Alonso Cotta
Keyword(s):  
Atomic Force Microscope ◽  
Living Cells ◽  
Adhesion Forces ◽  
Atomic Force ◽  
Calcium Blocker

scholarly journals RNA interactomics: recent advances and remaining challenges

F1000Research ◽  
2018 ◽  
Vol 7 ◽  
pp. 1824 ◽  
Author(s):  
Brigitte Schönberger ◽  
Christoph Schaal ◽  
Richard Schäfer ◽  
Björn Voß
Keyword(s):  
High Throughput ◽  
Rna Structure ◽  
Living Cells ◽  
Structure And Function ◽  
Cellular Processes ◽  
Recent Advances ◽  
Regulatory Systems ◽  
Rna Duplexes ◽  
And Function

Tight regulation of cellular processes is key to the development of complex organisms but also vital for simpler ones. During evolution, different regulatory systems have emerged, among them RNA-based regulation that is carried out mainly by intramolecular and intermolecular RNA–RNA interactions. However, methods for the transcriptome-wide detection of these interactions were long unavailable. Recently, three publications described high-throughput methods to directly detect RNA duplexes in living cells. This promises to enable in-depth studies of RNA-based regulation and will narrow the gaps in our understanding of RNA structure and function. In this review, we highlight the benefits of these methods and their commonalities and differences and, in particular, point to methodological shortcomings that hamper their wider application. We conclude by presenting ideas for how to overcome these problems and commenting on the prospects we see in this area of research.

Nanoscale Analysis of the Effect of Pathogenic Mutations on Polycystin-1

2010 ◽  
Author(s):  
Liang Ma ◽  
Meixiang Xu ◽  
Andres F. Oberhauser
Keyword(s):  
Single Molecule ◽  
Conformational Changes ◽  
Protein Interactions ◽  
Structure And Function ◽  
Eukaryotic Cells ◽  
Mechanical Forces ◽  
Force Microscopy ◽  
Physiological Conditions ◽  
Atomic Force ◽  
And Function

The activity of proteins and their complexes often involves the conversion of chemical energy (stored or supplied) into mechanical work through conformational changes. Mechanical forces are also crucial for the regulation of the structure and function of cells and tissues. Thus, the shape of eukaryotic cells is the result of cycles of mechano-sensing, mechano-transduction, and mechano-response. Recently developed single-molecule atomic force microscopy (AFM) techniques can be used to manipulate single molecules, both in real time and under physiological conditions, and are ideally suited to directly quantify the forces involved in both intra- and intermolecular protein interactions. In combination with molecular biology and computer simulations, these techniques have been applied to characterize the unfolding and refolding reactions in a variety of proteins, such as titin (an elastic mechano-sensing protein found in muscle) and polycystin-1 (PC1, a mechanosensor found in the kidney).

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