Optical Characteristics of Atomic Force Microscopy Tips for Single-Molecule Fluorescence Applications

ChemPhysChem ◽  
2005 ◽  
Vol 6 (5) ◽  
pp. 976-983 ◽  
Author(s):  
Alexander Gaiduk ◽  
Ralf Kühnemuth ◽  
Matthew Antonik ◽  
Claus A. M. Seidel
Keyword(s):  
Atomic Force Microscopy ◽  
Single Molecule ◽  
Optical Characteristics ◽  
Single Molecule Fluorescence ◽  
Force Microscopy ◽  
Atomic Force

Investigation of Perylene Photonic Wires by Combined Single-Molecule Fluorescence and Atomic Force Microscopy

2004 ◽  
Vol 116 (31) ◽  
pp. 4137-4141 ◽  
Author(s):  
Jordi Hernando ◽  
Pieter A. J. de Witte ◽  
Erik M. H.P van Dijk ◽  
Jeroen Korterik ◽  
Roeland J. M. Nolte ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Single Molecule ◽  
Single Molecule Fluorescence ◽  
Force Microscopy ◽  
Atomic Force ◽  
Photonic Wires

scholarly journals Single Molecule Fluorescence and Atomic Force Microscopy Studies of DNA Repair

2017 ◽  
Vol 112 (3) ◽  
pp. 7a
Author(s):  
Dorothy Erie ◽  
Kira Bradford ◽  
Hunter Wilkins ◽  
Jacqueline Bower ◽  
Zimeng Wang ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Dna Repair ◽  
Single Molecule ◽  
Single Molecule Fluorescence ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals Protein O-Fucosyltransferase 1 Undergoes Interdomain Flexibility in Solution

Molecules ◽  
2021 ◽  
Vol 26 (8) ◽  
pp. 2105
Author(s):  
Erandi Lira-Navarrete ◽  
María Carmen Pallarés ◽  
Fabio Castello ◽  
Maria J. Ruedas-Rama ◽  
Angel Orte ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Single Molecule ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Catalytic Cycle ◽  
Conformational Behavior ◽  
Single Molecule Fluorescence ◽  
Force Microscopy ◽  
Atomic Force ◽  
Dynamic Population

Protein O-fucosyltransferase 1 (PoFUT1) is a GT-B fold enzyme that fucosylates proteins containing EGF-like repeats. GT-B glycosyltransferases have shown a remarkable grade of plasticity adopting closed and open conformations as a way of tuning their catalytic cycle, a feature that has not been observed for PoFUT1. Here, we analyzed Caenorhabditis elegans PoFUT1 (CePoFUT1) conformational behavior in solution by atomic force microscopy (AFM) and single-molecule fluorescence resonance energy transfer (SMF-FRET). Our results show that this enzyme is very flexible and adopts mainly compact conformations and to a lesser extend a highly dynamic population that oscillates between compact and highly extended conformations. Overall, our experiments illustrate the inherent complexity of CePoFUT1 dynamics, which might play a role during its catalytic cycle.

Investigation of Perylene Photonic Wires by Combined Single-Molecule Fluorescence and Atomic Force Microscopy

2004 ◽  
Vol 43 (31) ◽  
pp. 4045-4049 ◽  
Author(s):  
Jordi Hernando ◽  
Pieter A. J. de Witte ◽  
Erik M. H.P van Dijk ◽  
Jeroen Korterik ◽  
Roeland J. M. Nolte ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Single Molecule ◽  
Single Molecule Fluorescence ◽  
Force Microscopy ◽  
Atomic Force ◽  
Photonic Wires

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
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