scholarly journals Self‐Assembly of Proteinaceous Shells around Positively Charged Gold Nanomaterials Enhances Colloidal Stability in High‐Ionic‐Strength Buffers

ChemBioChem ◽  
2019 ◽  
Vol 21 (1-2) ◽  
pp. 74-79
Author(s):  
Eita Sasaki ◽  
Ryan M. Dragoman ◽  
Shiksha Mantri ◽  
Dmitry N. Dirin ◽  
Maksym V. Kovalenko ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Self Assembly ◽  
Colloidal Stability ◽  
High Ionic Strength ◽  
Gold Nanomaterials ◽  
Positively Charged

The self-assembly of synthetic filaments of myosin isolated from Chaos carolinensis and Amoeba proteus

1977 ◽  
Vol 25 (1) ◽  
pp. 387-402
Author(s):  
J.S. Condeelis
Keyword(s):  
Ionic Strength ◽  
Self Assembly ◽  
Divalent Cations ◽  
Central Zone ◽  
Thick Filament ◽  
Amoeba Proteus ◽  
High Ionic Strength ◽  
Thick Filaments ◽  
Myosin Filaments ◽  
Low Ionic Strength

Synthetic myosin thick filaments were formed from preparations of electrophoretically homogeneous myosin isolated from Chaos carolinensis and Amoeba proteus when dialysed to physiological ionic strength and pH. Myosin dialysed directly against low ionic strength buffers formed native-like thick filaments in the presence and absence of exogenous divalent cations. The average dimensions of the synthetic filaments grown under these conditions were 455 nm long and 16 nm wide with a distinct bare central zone 174 nm long. Myosin predialysed against EGTA-EDTA solutions at high ionic strength and then dialysed to low ionic strength formed native-like filaments only in the presence of 1mM Mg2+. 1 mM Ca2+ could not be substituted for Mg2+ under these conditions to achieve native-like filaments. Filaments grown from predialysed myosin in the absence of Mg2+ resembled EGTA-dissociated myosin filaments observed in EGTA-treated cytoplasm and were highly branched, poorly formed filaments lacking a distinct bare central zone. The average dimensions of the filaments grown from predialysed myosin in the absence of Mg2+ were 328 nm long, 13 nm wide with a bare central zone 111 nm long. Under the conditions tested, myosin isolated from these amoebae did not demonstrate a divalent cation requirement for thick filament formation. The results obtained with myosin isolated from the 2 organisms were identical.

scholarly journals Vesicle Self-Assembly of Monoalkyl Amphiphiles under the Effects of High Ionic Strength, Extreme pH, and High Temperature Environments

Langmuir ◽  
2018 ◽  
Vol 34 (50) ◽  
pp. 15560-15568 ◽  
Author(s):  
Sarah E. Maurer ◽  
Kristian Tølbøl Sørensen ◽  
Zaki Iqbal ◽  
Jacqueline Nicholas ◽  
Kevin Quirion ◽  
...  
Keyword(s):  
High Temperature ◽  
Ionic Strength ◽  
Self Assembly ◽  
High Ionic Strength
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