Irreversible structural change of a dry ionic liquid under nanoconfinement

2015 ◽  
Vol 17 (20) ◽  
pp. 13613-13624 ◽  
Author(s):  
L. Andres Jurado ◽  
Hojun Kim ◽  
Andrea Arcifa ◽  
Antonella Rossi ◽  
Cecilia Leal ◽  
...  
Keyword(s):  
Ionic Liquid ◽  
Structural Change ◽  
Long Range ◽  
Liquid To Solid Transition

Repeatedly applied nanoconfinement of [HMIM] EtSO4 between mica surfaces induces a long-range liquid-to-solid transition that remains after confinement has been removed.

Long-Range Ordering of Ionic Liquid Fluid Films

Langmuir ◽  
2016 ◽  
Vol 32 (20) ◽  
pp. 5147-5154 ◽  
Author(s):  
Radhika S. Anaredy ◽  
Scott K. Shaw
Keyword(s):  
Ionic Liquid ◽  
Long Range ◽  
Fluid Films ◽  
Long Range Ordering

Comparing the void space and long-range structure of an ionic liquid with a neutral mixture of similar sized molecules

2020 ◽  
Vol 299 ◽  
pp. 112121 ◽  
Author(s):  
Ekaterina A. Shelepova ◽  
Dietmar Paschek ◽  
Ralf Ludwig ◽  
Nikolai N. Medvedev
Keyword(s):  
Ionic Liquid ◽  
Long Range ◽  
Void Space

Water-induced mica/ionic liquid interfacial nanostructure switches revealed by AFM

2020 ◽  
Vol 56 (95) ◽  
pp. 15064-15067
Author(s):  
Shuai Liu ◽  
Miangang Li ◽  
Jin Peng ◽  
Li Chen ◽  
Bingwei Mao ◽  
...  
Keyword(s):  
Ionic Liquid ◽  
Water Content ◽  
Long Range ◽  
Liquid Interface ◽  
Force Curve ◽  
Range Force

AFM force curve measurements reveal a long-range force switch from attraction to repulsion at the mica/ionic liquid interface due to the increase of water content.

Charge-Induced Long-Range Order in a Room-Temperature Ionic Liquid

Langmuir ◽  
2016 ◽  
Vol 32 (37) ◽  
pp. 9507-9512 ◽  
Author(s):  
Ke Ma ◽  
Romana Jarosova ◽  
Greg M. Swain ◽  
Gary J. Blanchard
Keyword(s):  
Ionic Liquid ◽  
Long Range ◽  
Room Temperature ◽  
Room Temperature Ionic Liquid ◽  
Range Order ◽  
Long Range Order

scholarly journals Structural variations in actins. Biochemical and immunological tools for probing the structure of rabbit skeletal-muscle and bovine aortic actins

1985 ◽  
Vol 231 (2) ◽  
pp. 363-368 ◽  
Author(s):  
J C Cavadore ◽  
C Roustan ◽  
Y Benyamin ◽  
M Boyer ◽  
J Haiech
Keyword(s):  
Skeletal Muscle ◽  
Structural Change ◽  
Long Range ◽  
Rabbit Skeletal Muscle ◽  
Terminal Part ◽  
Structural Variations ◽  
Sequence Variations ◽  
Structural Differences ◽  
Minor Sequence

Structural differences between skeletal-muscle and aortic actins were studied by using biochemical and immunological approaches. By using proteinase digestion we found that three regions of actin show structural differences: (a) in the C-terminal part, (b) the region around residue 227 and (c) the region around residue 167. By using antibodies specific to particular actin conformations we can discriminate between monomeric and filamentous forms of the two actins. Our results show that the minor sequence variations of the N- and C-terminal regions induce structural change in these regions, but also some long-range structural variations in other regions.

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