Resolving the High-Resolution Architecture, Assembly and Functional Repertoire of Bacterial Systems by in vitro Atomic Force Microscopy

2011 ◽  
pp. 71-97 ◽  
Author(s):  
Alexander Malkin
Keyword(s):  
Atomic Force Microscopy ◽  
High Resolution ◽  
Force Microscopy ◽  
Atomic Force ◽  
Bacterial Systems

scholarly journals Unraveling the Architecture and Structural Dynamics of Pathogens by High-Resolution in vitro Atomic Force Microscopy

2005 ◽  
Vol 11 (S03) ◽  
pp. 32-35 ◽  
Author(s):  
A. J. Malkin ◽  
M. Plomp ◽  
T. J. Leighton ◽  
A. McPherson ◽  
K. E. Wheeler
Keyword(s):  
Atomic Force Microscopy ◽  
High Resolution ◽  
Crystallographic Analysis ◽  
Human Pathogens ◽  
Force Microscopy ◽  
Environmental Resistance ◽  
Macromolecular Assemblies ◽  
Atomic Force ◽  
Internal Structures

Progress in structural biology very much depends upon the development of new high-resolution techniques and tools. Despite decades of study of viruses, bacteria and bacterial spores and their pressing importance in human medicine and biodefense, many of their structural properties are poorly understood. Thus, characterization and understanding of the architecture of protein surface and internal structures of pathogens is critical to elucidating mechanisms of disease, immune response, physicochemical properties, environmental resistance and development of countermeasures against bioterrorist agents. Furthermore, even though complete genome sequences are available for various pathogens, the structure-function relationships are not understood. Because of their lack of symmetry and heterogeneity, large human pathogens are often refractory to X-ray crystallographic analysis or reconstruction by cryo-electron microscopy (cryo-EM). An alternative high-resolution method to examine native structure of pathogens is atomic force microscopy (AFM), which allows direct visualization of macromolecular assemblies at near-molecular resolution. The capability to image single pathogen surfaces at nanometer scale in vitro would profoundly impact mechanistic and structural studies of Progress in structural biology very much depends upon the development of new high-resolution techniques and tools. Despite decades of study of viruses, bacteria and bacterial spores and their pressing importance in human medicine and biodefense, many of their structural properties are poorly understood. Thus, characterization and understanding of the architecture of protein surface and internal structures of pathogens is critical to elucidating mechanisms of disease, immune response, physicochemical properties, environmental resistance and development of countermeasures against bioterrorist agents. Furthermore, even though complete genome sequences are available for various pathogens, the structure-function relationships are not understood. Because of their lack of symmetry and heterogeneity, large human pathogens are often refractory to X-ray crystallographic analysis or reconstruction by cryo-electron microscopy (cryo-EM). An alternative high-resolution method to examine native structure of pathogens is atomic force microscopy (AFM), which allows direct visualization of macromolecular assemblies at near-molecular resolution. The capability to image single pathogen surfaces at nanometer scale in vitro would profoundly impact mechanistic and structural studies of pathogenesis, immunobiology, specific cellular processes, environmental dynamics and biotransformation.

Mapping in vitro local material properties of intact and disrupted virions at high resolution using multi-harmonic atomic force microscopy

Nanoscale ◽  
2013 ◽  
Vol 5 (11) ◽  
pp. 4729 ◽  
Author(s):  
Alexander Cartagena ◽  
Mercedes Hernando-Pérez ◽  
José L. Carrascosa ◽  
Pedro J. de Pablo ◽  
Arvind Raman
Keyword(s):  
Atomic Force Microscopy ◽  
High Resolution ◽  
Material Properties ◽  
Force Microscopy ◽  
Atomic Force ◽  
Local Material ◽  
Local Material Properties

scholarly journals Exploring Intramolecular Methyl–Methyl Coupling on a Metal Surface for Edge-Extended Graphene Nanoribbons

2021 ◽  
Vol 03 (02) ◽  
pp. 128-133
Author(s):  
Zijie Qiu ◽  
Qiang Sun ◽  
Shiyong Wang ◽  
Gabriela Borin Barin ◽  
Bastian Dumslaff ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Atomic Force Microscopy ◽  
High Resolution ◽  
Graphene Nanoribbons ◽  
Scanning Tunneling ◽  
Tunneling Microscopy ◽  
Force Microscopy ◽  
Methyl Methyl ◽  
Atomic Force ◽  
Edge Extension

Intramolecular methyl–methyl coupling on Au (111) is explored as a new on-surface protocol for edge extension in graphene nanoribbons (GNRs). Characterized by high-resolution scanning tunneling microscopy, noncontact atomic force microscopy, and Raman spectroscopy, the methyl–methyl coupling is proven to indeed proceed at the armchair edges of the GNRs, forming six-membered rings with sp3- or sp2-hybridized carbons.

Imaging of Xenopus laevis Oocyte Plasma Membrane in Physiological-Like Conditions by Atomic Force Microscopy

2013 ◽  
Vol 19 (5) ◽  
pp. 1358-1363 ◽  
Author(s):  
Massimo Santacroce ◽  
Federica Daniele ◽  
Andrea Cremona ◽  
Diletta Scaccabarozzi ◽  
Michela Castagna ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Plasma Membrane ◽  
High Resolution ◽  
Membrane Proteins ◽  
Xenopus Laevis ◽  
Functional Study ◽  
Xenopus Laevis Oocyte ◽  
Force Microscopy ◽  
Atomic Force ◽  
Afm Imaging

AbstractXenopus laevis oocytes are an interesting model for the study of many developmental mechanisms because of their dimensions and the ease with which they can be manipulated. In addition, they are widely employed systems for the expression and functional study of heterologous proteins, which can be expressed with high efficiency on their plasma membrane. Here we applied atomic force microscopy (AFM) to the study of the plasma membrane of X. laevis oocytes. In particular, we developed and optimized a new sample preparation protocol, based on the purification of plasma membranes by ultracentrifugation on a sucrose gradient, to perform a high-resolution AFM imaging of X. laevis oocyte plasma membrane in physiological-like conditions. Reproducible AFM topographs allowed visualization and dimensional characterization of membrane patches, whose height corresponds to a single lipid bilayer, as well as the presence of nanometer structures embedded in the plasma membrane and identified as native membrane proteins. The described method appears to be an applicable tool for performing high-resolution AFM imaging of X. laevis oocyte plasma membrane in a physiological-like environment, thus opening promising perspectives for studying in situ cloned membrane proteins of relevant biomedical/pharmacological interest expressed in this biological system.

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