scholarly journals Quantitative spectroscopy of single molecule interaction times

2021 ◽  
Author(s):  
Horst-Holger Boltz ◽  
Alexei Sirbu ◽  
Nina Stelzer ◽  
Martin Lohse ◽  
Christof Schütte ◽  
...  
Keyword(s):  
Single Molecule ◽  
Quantitative Spectroscopy ◽  
Molecule Interaction

scholarly journals Resolving the Dynamic Non-Covalent Interaction inside Membrane Protein Channel by Single-Molecule Interaction Spectrum

2018 ◽  
Author(s):  
Meng-Yin Li ◽  
Yi-Lun Ying ◽  
Xi-Xin Fu ◽  
Jie Yu ◽  
Shao-Chuang Liu ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Single Molecule ◽  
Ionic Current ◽  
Md Simulations ◽  
Energy Spectra ◽  
Membrane Channels ◽  
Non Covalent Interactions ◽  
Protein Channels ◽  
Covalent Interactions ◽  
Molecule Interaction

Millions of years of evolution have produced membrane protein channels capable of efficiently moving ions across the cell membrane. The underlying fundamental mechanisms that facilitate these actions greatly contribute to the weak non-covalent interactions. However, uncovering these dynamic interactions and its synergic network effects still remains challenging in both experimental techniques and molecule dynamics (MD) simulations. Here, we present a rational strategy that combines MD simulations and frequency-energy spectroscopy to identify and quantify the role of non-covalent interactions in carrier transport through membrane protein channels, as encoded in traditional single channel recording or ionic current. We employed wild-type aerolysin transporting of methylcytosine and cytosine as a model to explore the dynamic ionic signatures with non-stationary and non-linear frequency analysis. Our data illuminate that methylcytosine experiences strong non-covalent interactions with the aerolysin nanopore at Region 1 around R220 than cytosine, which produces characteristic frequency-energy spectra. Furthermore, we experimentally validate the obtained hypothesis from frequency-energy spectra by designing single-site mutation of K238G which creates significantly enhanced non-covalent interactions for the recognition of methylcytosine. The frequency-energy spectrum of ions flowing inside membrane channels constitutes a single-molecule interaction spectrum, which bridges the gap between traditional ionic current recording and the MD simulations, facilitating the qualitative and quantitive description of the non-covalent interactions inside membrane channels.

scholarly journals Solvent-molecule interaction induced gating of charge transport through single-molecule junctions

2020 ◽  
Vol 65 (11) ◽  
pp. 944-950 ◽  
Author(s):  
Zheng Tang ◽  
Songjun Hou ◽  
Qingqing Wu ◽  
Zhibing Tan ◽  
Jueting Zheng ◽  
...  
Keyword(s):  
Charge Transport ◽  
Single Molecule ◽  
Solvent Molecule ◽  
Single Molecule Junctions ◽  
Molecule Interaction

Single-molecule interaction force measurements of catechol analog monomers and synthesis of adhesive polymer using the results

2016 ◽  
Vol 48 (6) ◽  
pp. 715-721 ◽  
Author(s):  
Shougo Kinugawa ◽  
Siqian Wang ◽  
Shu Taira ◽  
Akihiko Tsuge ◽  
Daisaku Kaneko
Keyword(s):  
Single Molecule ◽  
Interaction Force ◽  
Force Measurements ◽  
Molecule Interaction

scholarly journals Single-molecule interaction microscopy reveals antibody binding kinetics

2020 ◽  
Author(s):  
Thilini Perera ◽  
Hirushi Gunasekara ◽  
Ying S. Hu
Keyword(s):  
Single Molecule ◽  
Antibody Binding ◽  
Binding Kinetics ◽  
Biomolecular Interactions ◽  
Single Molecule Imaging ◽  
Cellular Environment ◽  
Nanoscale Topography ◽  
Molecule Interaction ◽  
Limited Duration

Single-molecule imaging has provided new insights on weak transient biomolecular interactions with micromolar to millimolar affinity. However, the limited duration of observation has hindered the study of strong and reversible interactions with sub-nanomolar affinity. We report single-molecule interaction microscopy (SMIM), which combines point accumulation for imaging in nanoscale topography (PAINT) with extended imaging durations that enables the study of antibody binding kinetics in the cellular environment. SMIM revealed heterogeneous binding kinetics and the effect of concentration and antibody valency on the association and dissociation rates on antibody-antigen interactions in their cellular environments. We thereby demonstrate SMIM as a versatile single-molecule technique for studying strong, transient biomolecular interactions.

scholarly journals Resolving the Dynamic Non-Covalent Interaction inside Membrane Protein Channel by Single-Molecule Interaction Spectrum

2018 ◽  
Author(s):  
Meng-Yin Li ◽  
Yi-Lun Ying ◽  
Xi-Xin Fu ◽  
Jie Yu ◽  
Shao-Chuang Liu ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Single Molecule ◽  
Ionic Current ◽  
Md Simulations ◽  
Energy Spectra ◽  
Membrane Channels ◽  
Non Covalent Interactions ◽  
Protein Channels ◽  
Covalent Interactions ◽  
Molecule Interaction

Millions of years of evolution have produced membrane protein channels capable of efficiently moving ions across the cell membrane. The underlying fundamental mechanisms that facilitate these actions greatly contribute to the weak non-covalent interactions. However, uncovering these dynamic interactions and its synergic network effects still remains challenging in both experimental techniques and molecule dynamics (MD) simulations. Here, we present a rational strategy that combines MD simulations and frequency-energy spectroscopy to identify and quantify the role of non-covalent interactions in carrier transport through membrane protein channels, as encoded in traditional single channel recording or ionic current. We employed wild-type aerolysin transporting of methylcytosine and cytosine as a model to explore the dynamic ionic signatures with non-stationary and non-linear frequency analysis. Our data illuminate that methylcytosine experiences strong non-covalent interactions with the aerolysin nanopore at Region 1 around R220 than cytosine, which produces characteristic frequency-energy spectra. Furthermore, we experimentally validate the obtained hypothesis from frequency-energy spectra by designing single-site mutation of K238G which creates significantly enhanced non-covalent interactions for the recognition of methylcytosine. The frequency-energy spectrum of ions flowing inside membrane channels constitutes a single-molecule interaction spectrum, which bridges the gap between traditional ionic current recording and the MD simulations, facilitating the qualitative and quantitive description of the non-covalent interactions inside membrane channels.

scholarly journals A Single-Molecule Interaction Spectrum for Non-Covalent Interaction Inside Membrane Protein Channel

2019 ◽  
Vol 116 (3) ◽  
pp. 468a
Author(s):  
Meng-Yin Li ◽  
Yi-Lun Ying ◽  
Wei Tong ◽  
Yong-Jing Wan ◽  
Yi-Tao Long
Keyword(s):  
Membrane Protein ◽  
Single Molecule ◽  
Covalent Interaction ◽  
Protein Channel ◽  
Molecule Interaction
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