Prothrombin-membrane interaction. Effects of ionic strength, pH, and temperature

Robert M. Resnick; Gary L. Nelsestuen

doi:10.1021/bi00554a030

Hemoglobin - membrane interaction at physiological ionic strength and temperature

Life Sciences ◽

10.1016/0024-3205(87)90668-0 ◽

1987 ◽

Vol 41 (22) ◽

pp. 2429-2436 ◽

Cited By ~ 7

Author(s):

Gay L. Lilley ◽

Leslie W.-M. Fung

Keyword(s):

Ionic Strength ◽

Membrane Interaction

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Colloid–membrane interaction effects on flux decline during cross-flow ultrafiltration of colloidal silica on semi-ceramic membranes

Physical Chemistry Chemical Physics ◽

10.1039/b315220k ◽

2004 ◽

Vol 6 (7) ◽

pp. 1408-1412 ◽

Cited By ~ 19

Author(s):

P. Van der Meeren ◽

H. Saveyn ◽

S. Bogale Kassa ◽

W. Doyen ◽

R. Leysen

Keyword(s):

Colloidal Silica ◽

Cross Flow ◽

Ceramic Membranes ◽

Interaction Effects ◽

Membrane Interaction ◽

Flux Decline

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The ionic strength dependence of chromatin folding

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100081966 ◽

1978 ◽

Vol 36 (2) ◽

pp. 220-221

Author(s):

F. Thoma ◽

TH. Koller

Keyword(s):

Electron Microscopy ◽

Electron Microscope ◽

Ionic Strength ◽

Specimen Preparation ◽

Preparation Technique ◽

Carbon Supports ◽

Ionic Strength Dependence ◽

Chromatin Folding ◽

Strength Dependence ◽

Preparation Techniques

Under a variety of electron microscope specimen preparation techniques different forms of chromatin appearance can be distinguished: beads-on-a-string, a 100 Å nucleofilament, a 250 Å fiber and a compact 300 to 500 Å fiber.Using a standardized specimen preparation technique we wanted to find out whether there is any relation between these different forms of chromatin or not. We show that with increasing ionic strength a chromatin fiber consisting of a row of nucleo- somes progressively folds up into a solenoid-like structure with a diameter of about 300 Å.For the preparation of chromatin for electron microscopy the avoidance of stretching artifacts during adsorption to the carbon supports is of utmost importance. The samples are fixed with 0.1% glutaraldehyde at 4°C for at least 12 hrs. The material was usually examined between 24 and 48 hrs after the onset of fixation.

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Conformational Transitions in Escherichia coli Ribosomal RNAs as Visualized by Dedicated STEM

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100102961 ◽

1988 ◽

Vol 46 ◽

pp. 176-177

Author(s):

J.S. Wall ◽

V. Maridiyan ◽

S. Tumminia ◽

J. Hairifeld ◽

M. Boublik

Keyword(s):

Ionic Strength ◽

Three Dimensional ◽

Conformational Transitions ◽

Dark Field ◽

Dimensional Structure ◽

Ribosomal Rnas ◽

Field Mode ◽

Freeze Dried ◽

High Resolution Images ◽

Low Ionic Strength

The high contrast in the dark-field mode of dedicated STEM, specimen deposition by the wet film technique and low radiation dose (1 e/Å2) at -160°C make it possible to obtain high resolution images of unstained freeze-dried macromolecules with minimal structural distortion. Since the image intensity is directly related to the local projected mass of the specimen it became feasible to determine the molecular mass and mass distribution within individual macromolecules and from these data to calculate the linear density (M/L) and the radii of gyration.2 This parameter (RQ), reflecting the three-dimensional structure of the macromolecular particles in solution, has been applied to monitor the conformational transitions in E. coli 16S and 23S ribosomal RNAs in solutions of various ionic strength.In spite of the differences in mass (550 kD and 1050 kD, respectively), both 16S and 23S RNA appear equally sensitive to changes in buffer conditions. In deionized water or conditions of extremely low ionic strength both appear as filamentous structures (Fig. la and 2a, respectively) possessing a major backbone with protruding branches which are more frequent and more complex in 23S RNA (Fig. 2a).

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The three-dimensional structure of frozen-hydrated left- and right-handed forms of bacterial flagellar filaments from an identical serotype

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100143110 ◽

1986 ◽

Vol 44 ◽

pp. 298-299

Author(s):

S. Trachtenberg ◽

D. J. DeRosier

Keyword(s):

Ionic Strength ◽

Basal Body ◽

Three Dimensional ◽

Dimensional Structure ◽

Protein Species ◽

Liquid Environment ◽

Bacterial Flagellum ◽

Left And Right ◽

Rotary Motor ◽

Helical Parameters

The bacterial cell is propelled through the liquid environment by means of one or more rotating flagella. The bacterial flagellum is composed of a basal body (rotary motor), hook (universal coupler), and filament (propellor). The filament is a rigid helical assembly of only one protein species — flagellin. The filament can adopt different morphologies and change, reversibly, its helical parameters (pitch and hand) as a function of mechanical stress and chemical changes (pH, ionic strength) in the environment.

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