Measuring Interactions of DNA with Nanoporous Protein Crystals by Atomic Force Microscopy

Nanoscale ◽  
2021 ◽  
Author(s):  
Dafu Wang ◽  
Julius Stuart ◽  
Alec A Jones ◽  
Christopher Davis Snow ◽  
Matt Kipper
Keyword(s):  
Atomic Force Microscopy ◽  
Protein Crystals ◽  
Guest Molecules ◽  
Force Microscopy ◽  
Atomic Force ◽  
First Time

Crosslinked porous protein crystals are a new biomaterial that can be engineered to encapsulate, stabilize, and organize guest molecules, nanoparticles, and biological moieties. In this study, for the first time,...

Fusion Pore in Live Cells

Physiology ◽  
2002 ◽  
Vol 17 (6) ◽  
pp. 219-222 ◽  
Author(s):  
Bhanu P. Jena
Keyword(s):  
Atomic Force Microscopy ◽  
Live Cells ◽  
Fusion Pore ◽  
Secretory Cells ◽  
Secretory Vesicles ◽  
Force Microscopy ◽  
Atomic Force ◽  
Electrophysiological Measurements ◽  
First Time ◽  
Fusion Pores

Earlier electrophysiological measurements on live secretory cells suggested the presence of fusion pores at the plasma membrane, where secretory vesicles fuse to release vesicular contents. Recent studies using atomic force microscopy demonstrate for the first time the presence of the fusion pore and reveal its morphology and dynamics at near-nanometer resolution and in real time.

Force probing of protein crystals: An atomic force microscopy study

2000 ◽  
Vol 3 (4) ◽  
pp. 315-321 ◽  
Author(s):  
V. Mollica ◽  
A. Relini ◽  
R. Rolandi ◽  
M. Bolognesi ◽  
A. Gliozzi
Keyword(s):  
Atomic Force Microscopy ◽  
Microscopy Study ◽  
Protein Crystals ◽  
Atomic Force Microscopy Study ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals Reinforcement Mechanism of Carbon Black-Filled Rubber Nanocomposite as Revealed by Atomic Force Microscopy Nanomechanics

Polymers ◽  
2021 ◽  
Vol 13 (22) ◽  
pp. 3922
Author(s):  
Xiaobin Liang ◽  
Makiko Ito ◽  
Ken Nakajima
Keyword(s):  
Atomic Force Microscopy ◽  
Stress Distribution ◽  
Carbon Black ◽  
Stress Concentrations ◽  
Force Microscopy ◽  
Reinforcement Mechanism ◽  
Atomic Force ◽  
Filled Rubber ◽  
First Time ◽  
The Relationship

In this study, atomic force microscopy (AFM) nanomechanics were used to visualize the nanoscale stress distribution in carbon black (CB)-reinforced isoprene rubber (IR) vulcanizates at different elongations and quantitatively evaluate their volume fractions for the first time. The stress concentrations in the protofibrous structure (stress chains) that formed around the CB filler in CB-reinforced IR vulcanizates were directly observed at the nanoscale. The relationship between the local nanoscale stress distribution and macroscopic tensile properties was revealed based on the microscopic stress distribution and microscopic spatial structure. This study can help us gain insight into the microscopic reinforcement mechanism of carbon black-containing rubber composites.

scholarly journals Методы атомно-силовой микроскопии для исследования суперпротонных кристаллов

2020 ◽  
Vol 90 (11) ◽  
pp. 1843
Author(s):  
Р.В. Гайнутдинов ◽  
А.Л. Толстихина ◽  
Е.В. Селезнева ◽  
И.П. Макарова
Keyword(s):  
Atomic Force Microscopy ◽  
Surface Morphology ◽  
Ammonium Sulfate ◽  
Paraelectric Phase ◽  
Piezoelectric Response ◽  
Force Microscopy ◽  
Atomic Force ◽  
Microscopy Data ◽  
The Stability ◽  
First Time

Complex studies of new superprotonic crystals - acidic salts of potassium – ammonium sulfate (K1-x(NH4)x)3H(SO4)2, x ≥ 0.57 were carried out. Data on surface morphology, domain structure and conductivity of samples were obtained using atomic force microscopy. For the first time, the stability and degradation of the surface of superprotonic crystals were studied at the nanoscale. Based on piezoelectric response microscopy data, it was found that when the temperature decreased from 296 to 282 K, the (K0.43(NH4)0.57)3H(SO4)2 crystal transits from the paraelectric phase to the ferroelectric one.

scholarly journals The effect of Galleria mellonella hemolymph polypeptides on Legionella gormanii.

2014 ◽  
Vol 61 (1) ◽  
Author(s):  
Elżbieta Chmiel ◽  
Marta Palusinska-Szysz ◽  
Agnieszka Zdybicka-Barabas ◽  
Małgorzata Cytryńska ◽  
Paweł Mak
Keyword(s):  
Atomic Force Microscopy ◽  
Survival Rate ◽  
Galleria Mellonella ◽  
Community Acquired Pneumonia ◽  
Force Microscopy ◽  
Apolipophorin Iii ◽  
Atomic Force ◽  
Legionella Species ◽  
Induced Changes ◽  
First Time

Among Legionella species, which are recognized to be pathogenic for humans, L. gormanii is the second prevalent causative agent of community-acquired pneumonia after L. pneumophila. Anti-L. gormanii activity of Galleria mellonella hemolymph extract and apolipophorin III (apoLp-III) was examined. The extract and apoLp-III at the concentration 0.025 mg/ml caused 75% and 10% decrease of the bacteria survival rate, respectively. The apoLp-III-induced changes of the bacteria cell surface were analyzed for the first time by atomic force microscopy. Our studies demonstrated the powerful anti-Legionella effects of the insect defence polypeptides, which could be exploited in drugs design against these pathogens.

scholarly journals Polydisperse molecular architecture of connexin 26/30 heteromeric hemichannels revealed by atomic force microscopy imaging

2020 ◽  
Vol 295 (49) ◽  
pp. 16499-16509
Author(s):  
Pamela A. Naulin ◽  
Benjamin Lozano ◽  
Christian Fuentes ◽  
Yu Liu ◽  
Carla Schmidt ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Molecular Architecture ◽  
Microscopy Imaging ◽  
Force Microscopy ◽  
Atomic Force ◽  
Subunit Stoichiometry ◽  
Intercellular Channels ◽  
Atomic Force Microscopy Imaging ◽  
Gap Junctional ◽  
First Time

Connexin (Cx) protein forms hemichannels and gap junctional channels, which play diverse and profound roles in human physiology and diseases. Gap junctions are arrays of intercellular channels formed by the docking of two hemichannels from adjacent cells. Each hexameric hemichannel contains the same or different Cx isoform. Although homomeric Cxs forms have been largely described functionally and structurally, the stoichiometry and arrangement of heteromeric Cx channels remain unknown. The latter, however, are widely expressed in human tissues and variation might have important implications on channel function. Investigating properties of heteromeric Cx channels is challenging considering the high number of potential subunit arrangements and stoichiometries, even when only combining two Cx isoforms. To tackle this problem, we engineered an HA tag onto Cx26 or Cx30 subunits and imaged hemichannels that were liganded by Fab-epitope antibody fragments via atomic force microscopy. For Cx26-HA/Cx30 or Cx30-HA/Cx26 heteromeric channels, the Fab-HA binding distribution was binomial with a maximum of three Fab-HA bound. Furthermore, imaged Cx26/Cx30-HA triple liganded by Fab-HA showed multiple arrangements that can be derived from the law of total probabilities. Atomic force microscopy imaging of ringlike structures of Cx26/Cx30-HA hemichannels confirmed these findings and also detected a polydisperse distribution of stoichiometries. Our results indicate a dominant subunit stoichiometry of 3Cx26:3Cx30 with the most abundant subunit arrangement of Cx26-Cx26-Cx30-Cx26-Cx30-Cx30. To our knowledge, this is the first time that the molecular architecture of heteromeric Cx channels has been revealed, thus providing the basis to explore the functional effect of these channels in biology.

Protein Crystals as Scanned Probes for Recognition Atomic Force Microscopy

Nano Letters ◽  
2005 ◽  
Vol 5 (12) ◽  
pp. 2418-2421 ◽  
Author(s):  
Nissanka S. Wickremasinghe ◽  
Jason H. Hafner
Keyword(s):  
Atomic Force Microscopy ◽  
Protein Crystals ◽  
Force Microscopy ◽  
Atomic Force ◽  
Scanned Probes
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