Compact and stable SNAP ligand-conjugated quantum dots as a fluorescent probe for single-molecule imaging of dynein motor protein

2015 ◽  
Vol 51 (80) ◽  
pp. 14836-14839 ◽  
Author(s):  
Tatsuya Ohyanagi ◽  
Tomohiro Shima ◽  
Yasushi Okada ◽  
Yoshikazu Tsukasaki ◽  
Akihito Komatsuzaki ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Fluorescent Probe ◽  
Single Molecule ◽  
Colloidal Stability ◽  
Motor Protein ◽  
Single Molecule Imaging ◽  
Dynein Motor ◽  
Wide Range

Compact SNAP ligand-conjugated quantum dots (<10 nm) with high colloidal stability over a wide range of pH (5–9) are presented as a fluorescent probe for single-molecule imaging of dynein motor protein.

scholarly journals Single Molecule Imaging with Stable 6 NM Quantum Dots

2012 ◽  
Vol 102 (3) ◽  
pp. 182a
Author(s):  
En Cai ◽  
Katie Wilson ◽  
Pinghua Ge ◽  
Marco Tjioe ◽  
David G. Fernig ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Single Molecule ◽  
Single Molecule Imaging

Compact Halo-Ligand-Conjugated Quantum Dots for Multicolored Single-Molecule Imaging of Overcrowding GPCR Proteins on Cell Membranes

Small ◽  
2014 ◽  
Vol 11 (12) ◽  
pp. 1396-1401 ◽  
Author(s):  
Akihito Komatsuzaki ◽  
Tatsuya Ohyanagi ◽  
Yoshikazu Tsukasaki ◽  
Yukihiro Miyanaga ◽  
Masahiro Ueda ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Single Molecule ◽  
Cell Membranes ◽  
Single Molecule Imaging

scholarly journals Stable, small, specific, low-valency quantum dots for single-molecule imaging

Nanoscale ◽  
2018 ◽  
Vol 10 (9) ◽  
pp. 4406-4414 ◽  
Author(s):  
Jungmin Lee ◽  
Xinyi Feng ◽  
Ou Chen ◽  
Moungi G. Bawendi ◽  
Jun Huang
Keyword(s):  
Quantum Dots ◽  
Single Cell ◽  
Single Molecule ◽  
Single Molecule Imaging

Small, specific, low-valency quantum dots for single-cell and single-molecule imaging.

scholarly journals Imaging: Compact Halo-Ligand-Conjugated Quantum Dots for Multicolored Single-Molecule Imaging of Overcrowding GPCR Proteins on Cell Membranes (Small 12/2015)

Small ◽  
2015 ◽  
Vol 11 (12) ◽  
pp. 1358-1358
Author(s):  
Akihito Komatsuzaki ◽  
Tatsuya Ohyanagi ◽  
Yoshikazu Tsukasaki ◽  
Yukihiro Miyanaga ◽  
Masahiro Ueda ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Single Molecule ◽  
Cell Membranes ◽  
Single Molecule Imaging

scholarly journals Multispecies Single Molecule Imaging With Quantum Dots

2009 ◽  
Vol 96 (3) ◽  
pp. 283a
Author(s):  
Christoffer Lagerholm ◽  
Eva Arnspang Christensen ◽  
Mathias Lysemose Clausen ◽  
Pasad Kulatunga
Keyword(s):  
Quantum Dots ◽  
Single Molecule ◽  
Single Molecule Imaging

scholarly journals Three-color single-molecule imaging reveals conformational dynamics of dynein undergoing motility

2020 ◽  
Author(s):  
Stefan Niekamp ◽  
Nico Stuurman ◽  
Nan Zhang ◽  
Ronald D. Vale
Keyword(s):  
Single Molecule ◽  
Conformational Changes ◽  
In Silico ◽  
Conformational Transition ◽  
Conformational Dynamics ◽  
Motor Protein ◽  
Single Molecule Imaging ◽  
Microtubule Binding ◽  
Binding Domains ◽  
Single Molecule Studies

The motor protein dynein undergoes coordinated conformational changes of its domains during motility along microtubules. Previous single-molecule studies analyzed the motion of the AAA rings of the dynein homodimer, but not the distal microtubule binding domains (MTBD) that step along the track. Here, we simultaneously tracked two MTBDs and one AAA ring of a single dynein, as it undergoes hundreds of steps with nanometer precision using three-color imaging. We show that the AAA ring and the MTBDs do not always step simultaneously and can take different sized steps. This variability in the movement between AAA ring and MTBD results in an unexpectedly large number of conformational states of dynein during motility. Extracting data on conformational transition biases, we could accurately model dynein stepping in silico. Our results reveal that the flexibility between major dynein domains is critical for dynein motility.

scholarly journals Three-color single-molecule imaging reveals conformational dynamics of dynein undergoing motility

2021 ◽  
Vol 118 (31) ◽  
pp. e2101391118
Author(s):  
Stefan Niekamp ◽  
Nico Stuurman ◽  
Nan Zhang ◽  
Ronald D. Vale
Keyword(s):  
Single Molecule ◽  
Conformational Changes ◽  
In Silico ◽  
Conformational Transition ◽  
Conformational Dynamics ◽  
Motor Protein ◽  
Single Molecule Imaging ◽  
Microtubule Binding ◽  
Binding Domains ◽  
Single Molecule Studies

The motor protein dynein undergoes coordinated conformational changes of its domains during motility along microtubules. Previous single-molecule studies analyzed the motion of the AAA rings of the dynein homodimer, but not the distal microtubule-binding domains (MTBDs) that step along the track. Here, we simultaneously tracked with nanometer precision two MTBDs and one AAA ring of a single dynein as it underwent hundreds of steps using three-color imaging. We show that the AAA ring and the MTBDs do not always step simultaneously and can take differently sized steps. This variability in the movement between the AAA ring and MTBDs results in an unexpectedly large number of conformational states of dynein during motility. Extracting data on conformational transition biases, we could accurately model dynein stepping in silico. Our results reveal that the flexibility between major dynein domains is critical for dynein motility.

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