scholarly journals Chemical structure imaging of a single molecule by atomic force microscopy at room temperature

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Kota Iwata ◽  
Shiro Yamazaki ◽  
Pingo Mutombo ◽  
Prokop Hapala ◽  
Martin Ondráček ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Single Molecule ◽  
Chemical Structure ◽  
Room Temperature ◽  
Force Microscopy ◽  
Atomic Force

Atomic Force Microscopy (AFM) for Topography and Recognition Imaging at Single Molecule Level

2013 ◽  
pp. 102-112
Author(s):  
Memed Duman ◽  
Andreas Ebner ◽  
Christian Rankl ◽  
Jilin Tang ◽  
Lilia A. Chtcheglova ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Single Molecule ◽  
Single Molecule Level ◽  
Force Microscopy ◽  
Atomic Force ◽  
Recognition Imaging

scholarly journals Atomic Force Microscopy Investigation of the Interactions between the MCM Helicase and DNA

Materials ◽  
2021 ◽  
Vol 14 (3) ◽  
pp. 687
Author(s):  
Amna Abdalla Mohammed Khalid ◽  
Pietro Parisse ◽  
Barbara Medagli ◽  
Silvia Onesti ◽  
Loredana Casalis
Keyword(s):  
Atomic Force Microscopy ◽  
Nucleic Acid ◽  
Single Molecule ◽  
Protein Complex ◽  
The Other ◽  
Contour Length ◽  
Force Microscopy ◽  
Atomic Force ◽  
Mcm Complex ◽  
Dna Double Helix

The MCM (minichromosome maintenance) protein complex forms an hexameric ring and has a key role in the replication machinery of Eukaryotes and Archaea, where it functions as the replicative helicase opening up the DNA double helix ahead of the polymerases. Here, we present a study of the interaction between DNA and the archaeal MCM complex from Methanothermobacter thermautotrophicus by means of atomic force microscopy (AFM) single molecule imaging. We first optimized the protocol (surface treatment and buffer conditions) to obtain AFM images of surface-equilibrated DNA molecules before and after the interaction with the protein complex. We discriminated between two modes of interaction, one in which the protein induces a sharp bend in the DNA, and one where there is no bending. We found that the presence of the MCM complex also affects the DNA contour length. A possible interpretation of the observed behavior is that in one case the hexameric ring encircles the dsDNA, while in the other the nucleic acid wraps on the outside of the ring, undergoing a change of direction. We confirmed this topographical assignment by testing two mutants, one affecting the N-terminal β-hairpins projecting towards the central channel, and thus preventing DNA loading, the other lacking an external subdomain and thus preventing wrapping. The statistical analysis of the distribution of the protein complexes between the two modes, together with the dissection of the changes of DNA contour length and binding angle upon interaction, for the wild type and the two mutants, is consistent with the hypothesis. We discuss the results in view of the various modes of nucleic acid interactions that have been proposed for both archaeal and eukaryotic MCM complexes.

Substrate Specificity of Sugar Transport by Rabbit SGLT1:  Single-Molecule Atomic Force Microscopy versus Transport Studies†

Biochemistry ◽  
2007 ◽  
Vol 46 (10) ◽  
pp. 2797-2804 ◽  
Author(s):  
Theeraporn Puntheeranurak ◽  
Barbara Wimmer ◽  
Francisco Castaneda ◽  
Hermann J. Gruber ◽  
Peter Hinterdorfer ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Substrate Specificity ◽  
Single Molecule ◽  
Sugar Transport ◽  
Force Microscopy ◽  
Atomic Force ◽  
Transport Studies

Open the door to the atomic world by single-molecule atomic force microscopy

Matter ◽  
2021 ◽  
Vol 4 (4) ◽  
pp. 1189-1223
Author(s):  
Siyuan Fang ◽  
Yun Hang Hu
Keyword(s):  
Atomic Force Microscopy ◽  
Single Molecule ◽  
Force Microscopy ◽  
Atomic Force

ATOMIC FORCE MICROSCOPY AND XRD ANALYSIS OF SILVER FILMS DEPOSITED BY THERMAL EVAPORATION

2006 ◽  
Vol 20 (02) ◽  
pp. 217-231 ◽  
Author(s):  
MUHAMMAD MAQBOOL ◽  
TAHIRZEB KHAN
Keyword(s):  
Atomic Force Microscopy ◽  
Grain Size ◽  
Surface Characterization ◽  
Room Temperature ◽  
Thermal Evaporation ◽  
Xrd Analysis ◽  
Force Microscopy ◽  
Atomic Force ◽  
Average Grain Size ◽  
20 Nm

Thin films of pure silver were deposited on glass substrate by thermal evaporation process at room temperature. Surface characterization of the films was performed using X-ray diffraction (XRD) and atomic force microscopy (AFM). Thickness of the films varied between 20 nm and 72.8 nm. XRD analysis provided a sharp peak at 38.75° from silver. These results indicated that the films deposited on glass substrates at room temperature are crystalline. Three-dimension and top view pictures of the films were obtained by AFM to study the grain size and its dependency on various factors. Average grain size increased with the thickness of the deposited films. A minimum grain size of 8 nm was obtained for 20 nm thick films, reaching 41.9 nm when the film size reaches 60 nm. Grain size was calculated from the information provided by the XRD spectrum and averaging method. We could not find any sequential variation in the grain size with the growth rate.

Reverse Engineering of an Affinity-Switchable Molecular Interaction Characterized by Atomic Force Microscopy Single-Molecule Force Spectroscopy†

Langmuir ◽  
2008 ◽  
Vol 24 (4) ◽  
pp. 1365-1370 ◽  
Author(s):  
Dario Anselmetti ◽  
Frank Wilco Bartels ◽  
Anke Becker ◽  
Björn Decker ◽  
Rainer Eckel ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Reverse Engineering ◽  
Single Molecule ◽  
Molecular Interaction ◽  
Force Spectroscopy ◽  
Single Molecule Force Spectroscopy ◽  
Force Microscopy ◽  
Atomic Force
Sign in / Sign up

Export Citation Format

Share Document