Polyacrylamide hydrogels for stone restoration: Effect of salt solutions on swelling/deswelling degree and dynamic correlation length

Microrheology is used to measure the length scale dependent mechanical response of F-actin gels. The dynamic correlation length thus measured has a non-trivial dependence on the actin filament length.

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Dynamic correlation length growth in superspin glass: Bridging experiments and simulations

Applied Physics Letters ◽

10.1063/1.4769840 ◽

2012 ◽

Vol 101 (24) ◽

pp. 242409 ◽

Cited By ~ 15

Author(s):

S. Nakamae ◽

C. Crauste-Thibierge ◽

D. L'Hôte ◽

E. Vincent ◽

E. Dubois ◽

...

Keyword(s):

Correlation Length ◽

Dynamic Correlation ◽

Length Growth ◽

Superspin Glass

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Dynamic correlation length scales under isochronal conditions

The Journal of Chemical Physics ◽

10.1063/1.4907371 ◽

2015 ◽

Vol 142 (6) ◽

pp. 064504 ◽

Cited By ~ 27

Author(s):

R. Casalini ◽

D. Fragiadakis ◽

C. M. Roland

Keyword(s):

Correlation Length ◽

Length Scales ◽

Dynamic Correlation

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Isomorphous replacement in electron diffraction of wet crystals of rat hemoglobin

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100075968 ◽

1983 ◽

Vol 41 ◽

pp. 446-447

Author(s):

William F. Tivol ◽

Murray Vernon King ◽

D. F. Parsons

Keyword(s):

Electron Diffraction ◽

Heavy Atom ◽

Isomorphous Substitution ◽

X Ray Diffraction ◽

Salt Solutions ◽

X Ray ◽

Isomorphous Replacement ◽

Structure Factors ◽

Diffraction Structure ◽

The Mean

Feasibility of isomorphous substitution in electron diffraction is supported by a calculation of the mean alteration of the electron-diffraction structure factors for hemoglobin crystals caused by substituting two mercury atoms per molecule, following Green, Ingram & Perutz, but with allowance for the proportionality of f to Z3/4 for electron diffraction. This yields a mean net change in F of 12.5%, as contrasted with 22.8% for x-ray diffraction.Use of the hydration chamber in electron diffraction opens prospects for examining many proteins that yield only very thin crystals not suitable for x-ray diffraction. Examination in the wet state avoids treatments that could cause translocation of the heavy-atom labels or distortion of the crystal. Combined with low-fluence techniques, it enables study of the protein in a state as close to native as possible.We have undertaken a study of crystals of rat hemoglobin by electron diffraction in the wet state. Rat hemoglobin offers a certain advantage for hydration-chamber work over other hemoglobins in that it can be crystallized from distilled water instead of salt solutions.

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Bulk standards for low-temperature biological x-ray microanalysis

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100111525 ◽

1984 ◽

Vol 42 ◽

pp. 282-283

Author(s):

P. Echlin ◽

M. McKoon ◽

E.S. Taylor ◽

C.E. Thomas ◽

K.L. Maloney ◽

...

Keyword(s):

Phase Separation ◽

Low Temperature ◽

Analytical Method ◽

Salt Solutions ◽

Absolute Concentration ◽

Cooling Process ◽

X Ray ◽

The Absolute ◽

Analytical Procedures ◽

Electrical Conductors

Although sections of frozen salt solutions have been used as standards for x-ray microanalysis, such solutions are less useful when analysed in the bulk form. They are poor thermal and electrical conductors and severe phase separation occurs during the cooling process. Following a suggestion by Whitecross et al we have made up a series of salt solutions containing a small amount of graphite to improve the sample conductivity. In addition, we have incorporated a polymer to ensure the formation of microcrystalline ice and a consequent homogenity of salt dispersion within the frozen matrix. The mixtures have been used to standardize the analytical procedures applied to frozen hydrated bulk specimens based on the peak/background analytical method and to measure the absolute concentration of elements in developing roots.

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