The Influence of Oxygen-Radicals on the Mechanisms of Conformational Changes and Denaturation of Haemoglobin Induced by UV Irradiation

Molecules embedded in low-temperature matrices experience conformer interconversion processes due to IR- (or UV-)irradiation. This paper summarizes the known IR-induced conformational changes, of which the majority has been studied by using broad-band sources provided with filters. We focus at the thermal and IR-photochemical methods in obtaining information of conformational energetics of matrix isolated molecules, at the usefulness of ab initio calculations in assigning the spectra of conformers involved and in finding the reaction path on the ground state surface. The data obtained from a number of molecules is used to discuss possible mechanisms in both intramolecularly hydrogen-bonded and non-bonded molecules. Also possible indications of mode-selective phenomena in these processes are dealt with. In addition, common trends found for photorotamerization in different hosts are discussed.

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Influence of Calcium Ions on the Plant Cell Surface: Membrane Fusions and Conformational Changes

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100050780 ◽

1974 ◽

Vol 32 ◽

pp. 154-155

Author(s):

D. James Morré ◽

Charles E. Bracker ◽

William J. VanDerWoude

Keyword(s):

Cell Wall ◽

Cell Surface ◽

Conformational Changes ◽

Calcium Ions ◽

Surface Membrane ◽

Carboxyl Groups ◽

Cross Linking ◽

Ultrastructural Evidence ◽

Glycine Max L ◽

Wall Extensibility

Calcium ions in the concentration range 5-100 mM inhibit auxin-induced cell elongation and wall extensibility of plant stems. Inhibition of wall extensibility requires that the tissue be living; growth inhibition cannot be explained on the basis of cross-linking of carboxyl groups of cell wall uronides by calcium ions. In this study, ultrastructural evidence was sought for an interaction of calcium ions with some component other than the wall at the cell surface of soybean (Glycine max (L.) Merr.) hypocotyls.

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Role of spectrin in membrane fusion and in shape change of human erythrocyte ghost

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100082509 ◽

1978 ◽

Vol 36 (2) ◽

pp. 328-329

Author(s):

Hideo Hayashi ◽

Yoshikazu Hirai ◽

John T. Penniston

Keyword(s):

Conformational Changes ◽

Human Erythrocyte ◽

Shape Change ◽

Membrane Surface ◽

Slight Modification ◽

Active Role ◽

Main Role ◽

Bank Blood ◽

Human Erythrocyte Ghost

Spectrin is a membrane associated protein most of which properties have been tentatively elucidated. A main role of the protein has been assumed to give a supporting structure to inside of the membrane. As reported previously, however, the isolated spectrin molecule underwent self assemble to form such as fibrous, meshwork, dispersed or aggregated arrangements depending upon the buffer suspended and was suggested to play an active role in the membrane conformational changes. In this study, the role of spectrin and actin was examined in terms of the molecular arrangements on the erythrocyte membrane surface with correlation to the functional states of the ghosts.Human erythrocyte ghosts were prepared from either freshly drawn or stocked bank blood by the method of Dodge et al with a slight modification as described before. Anti-spectrin antibody was raised against rabbit by injection of purified spectrin and partially purified.

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Pinocytotic-Like Forms of Mitochondria From Rat Anterior Pituitary

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100100470 ◽

1968 ◽

Vol 26 ◽

pp. 146-147

Author(s):

Burton B. Silver

Keyword(s):

Electron Micrographs ◽

Conformational Changes ◽

Anterior Pituitary ◽

Dynamic State ◽

Surrounding Cell ◽

The Matrix ◽

The Moment ◽

Cell Medium ◽

Sectioned Tissue ◽

State Of Activity

Sectioned tissue rarely indicates evidence of what is probably a highly dynamic state of activity in mitochondria which have been reported to undergo a variety of movements such as streaming, divisions and coalescence. Recently, mitochondria from the rat anterior pituitary have been fixed in a variety of configurations which suggest that conformational changes were occurring at the moment of fixation. Pinocytotic-like vacuoles which may be taking in or expelling materials from the surrounding cell medium, appear to be forming in some of the mitochondria. In some cases, pores extend into the matrix of the mitochondria. In other forms, the remains of what seems to be pinched off vacuoles are evident in the mitochondrial interior. Dense materials, resembling secretory droplets, appear at the junction of the pores and the cytoplasm. The droplets are similar to the secretory materials commonly identified in electron micrographs of the anterior pituitary.

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Electron Microscopy and image reconstruction reveal the structural basis for spectrin's elastic properties

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100122952 ◽

1992 ◽

Vol 50 (1) ◽

pp. 510-511

Author(s):

Amy M. McGough ◽

Robert Josephs

Keyword(s):

Electron Microscopy ◽

Elastic Properties ◽

Conformational Changes ◽

Quaternary Structure ◽

Three Dimensional ◽

Membrane Skeleton ◽

Projection Algorithm ◽

Structural Basis ◽

Iterative Approximation ◽

Membrane Skeletons

The remarkable deformability of the erythrocyte derives in large part from the elastic properties of spectrin, the major component of the membrane skeleton. It is generally accepted that spectrin's elasticity arises from marked conformational changes which include variations in its overall length (1). In this work the structure of spectrin in partially expanded membrane skeletons was studied by electron microscopy to determine the molecular basis for spectrin's elastic properties. Spectrin molecules were analysed with respect to three features: length, conformation, and quaternary structure. The results of these studies lead to a model of how spectrin mediates the elastic deformation of the erythrocyte.Membrane skeletons were isolated from erythrocyte membrane ghosts, negatively stained, and examined by transmission electron microscopy (2). Particle lengths and end-to-end distances were measured from enlarged prints using the computer program MACMEASURE. Spectrin conformation (straightness) was assessed by calculating the particles’ correlation length by iterative approximation (3). Digitised spectrin images were correlation averaged or Fourier filtered to improve their signal-to-noise ratios. Three-dimensional reconstructions were performed using a suite of programs which were based on the filtered back-projection algorithm and executed on a cluster of Microvax 3200 workstations (4).

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Protein-induced conformational changes in 16S rRNA during assembly of the Escherichia Coli 30S ribosomal subunit: A STEM study

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100128833 ◽

1987 ◽

Vol 45 ◽

pp. 910-911

Author(s):

M. Boublik ◽

V. Mandiyan ◽

J.F. Hainfeld ◽

J.S. Wall

Keyword(s):

16S Rrna ◽

Conformational Changes ◽

Ribosomal Proteins ◽

Structural Changes ◽

Ribosomal Subunit ◽

Compact Structure ◽

E Coli ◽

Freeze Dried ◽

16S Rna ◽

30S Subunit

The aim of this study is to understand the mechanism of 16S rRNA folding into the compact structure of the small 30S subunit of E. coli ribosome. The assembly of the 30S E. coli ribosomal subunit is a sequence of specific interactions of 16S rRNA with 21 ribosomal proteins (S1-S21). Using dedicated high resolution STEM we have monitored structural changes induced in 16S rRNA by the proteins S4, S8, S15 and S20 which are involved in the initial steps of 30S subunit assembly. S4 is the first protein to bind directly and stoichiometrically to 16S rRNA. Direct binding also occurs individually between 16S RNA and S8 and S15. However, binding of S20 requires the presence of S4 and S8. The RNA-protein complexes are prepared by the standard reconstitution procedure, dialyzed against 60 mM KCl, 2 mM Mg(OAc)2, 10 mM-Hepes-KOH pH 7.5 (Buffer A), freeze-dried and observed unstained in dark field at -160°.

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Oxygen radicals participate in alloxan-induced pulmonary EDEMA

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100159047 ◽

1990 ◽

Vol 48 (3) ◽

pp. 298-299

Author(s):

Tomoo Kawada ◽

Michio Arakawa ◽

Kenjiro Kambara ◽

Takashi Segawa ◽

Fumio Ando ◽

...

Keyword(s):

Pulmonary Edema ◽

Oxygen Radicals ◽

Bolus Injection ◽

Physiological Saline ◽

Baseline Period ◽

Alveolar Epithelial Cells ◽

Control Group ◽

Intervention Period ◽

Lung Water ◽

Electron Microscopic

We know that alloxan causes increased-permeability pulmonary edema and that alloxan generates oxygen radicals (H2O2, O2−, ·OH) in blood. Therefore, we hypothesize that alloxan-generated oxygen radicals damage pulmonary capillary endothelial cells, and, possibly, alveolar epithelial cells as well. We examined whether oxygen radical scavengers, such as catalase or dimethylsulfoxide (DMSO), protected against alloxaninduced pulmonary edema.Five dogs in each following group were anesthetized: control group: physiological saline (20ml/kg/h); alloxan group: physiological saline + alloxan (75mg/kg) bolus injection at the beginning of the experiment; catalase group: physiological saline + catalase (150,000u/kg) bolus injection before injection of alloxan; DMSO group: physiological saline + DMSO (0.4mg/kg) bolus injection before alloxan. All dogs had 30-min baseline period and 3-h intervention period. Hemodynamics and circulating substances were measured at the specific points of time. At the end of intervention period, the dogs were killed and had the lungs removed for electron microscopic study and lung water measurement with direct destructive method.

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Criteria for the evaluation of low-temperature Scanning Electron Microscopy

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100145820 ◽

1986 ◽

Vol 44 ◽

pp. 902-903

Author(s):

Alan Beckett

Keyword(s):

Electron Microscopy ◽

Scanning Electron Microscopy ◽

Low Temperature ◽

Conformational Changes ◽

Chemical Vapour ◽

List Type ◽

Dimensional Changes ◽

Critical Point Drying ◽

Temperature Scanning ◽

Scanning Electron

Low temperature scanning electron microscopy (LTSEM) has been evaluated with special reference to its application to the study of morphology and development in microorganisms. A number of criteria have been considered and have proved valuable in assessing the standard of results achieved. To further aid our understanding of these results, it has been necessary to compare those obtained by LTSEM with those from more conventional preparatory procedures such as 1) chemical fixation, dehydration and critical point-drying; 2) freeze-drying with or without chemical vapour fixation before hand.The criteria used for assessing LTSEM for the above purposes are as follows: 1)Specimen immobilization and stabilization2)General preservation of external morphology3)General preservation of internal morphology4)Exposure to solvents5)Overall dimensional changes6)Cell surface texture7)Differential conformational changes8)Etching frozen-hydrated material9)Beam damage10)Specimen resolution11)Specimen life

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