scholarly journals Effect of Self-Association on the Structural Organization of Partially Folded Proteins: Inactivated Actin

1999 ◽  
Vol 77 (5) ◽  
pp. 2788-2800 ◽  
Author(s):  
Irina M. Kuznetsova ◽  
Alexander G. Biktashev ◽  
Sofia Yu. Khaitlina ◽  
Konstantin S. Vassilenko ◽  
Konstantin K. Turoverov ◽  
...  
Keyword(s):  
Structural Organization ◽  
Folded Proteins ◽  
Self Association

scholarly journals N-terminal domain of the architectural protein CTCF has similar structural organization and ability to self-association in bilaterian organisms

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Artem Bonchuk ◽  
Sofia Kamalyan ◽  
Sofia Mariasina ◽  
Konstantin Boyko ◽  
Vladimir Popov ◽  
...  
Keyword(s):  
Structural Organization ◽  
Terminal Domain ◽  
Self Association ◽  
Architectural Protein

Structural organization of escherichia coli ribosomes as determined by immuno electron microscopy

1978 ◽  
Vol 36 (2) ◽  
pp. 166-167 ◽  
Author(s):  
G. Stöffler ◽  
R.W. Bald ◽  
J. Dieckhoff ◽  
H. Eckhard ◽  
R. Lührmann ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Ribosomal Subunit ◽  
Spatial Arrangement ◽  
Small Subunit ◽  
Antibody Binding ◽  
Immuno Electron Microscopy

A central step towards an understanding of the structure and function of the Escherichia coli ribosome, a large multicomponent assembly, is the elucidation of the spatial arrangement of its 54 proteins and its three rRNA molecules. The structural organization of ribosomal components has been investigated by a number of experimental approaches. Specific antibodies directed against each of the 54 ribosomal proteins of Escherichia coli have been performed to examine antibody-subunit complexes by electron microscopy. The position of the bound antibody, specific for a particular protein, can be determined; it indicates the location of the corresponding protein on the ribosomal surface.The three-dimensional distribution of each of the 21 small subunit proteins on the ribosomal surface has been determined by immuno electron microscopy: the 21 proteins have been found exposed with altogether 43 antibody binding sites. Each one of 12 proteins showed antibody binding at remote positions on the subunit surface, indicating highly extended conformations of the proteins concerned within the 30S ribosomal subunit; the remaining proteins are, however, not necessarily globular in shape (Fig. 1).

Ribosome Structural Organization

1974 ◽  
Vol 32 ◽  
pp. 332-333
Author(s):  
James A. Lake
Keyword(s):  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Small Subunit ◽  
Structural Studies ◽  
X Ray Diffraction ◽  
Specific Antibodies ◽  
X Ray ◽  
E Coli ◽  
Complete Sequences

The understanding of ribosome structure has advanced considerably in the last several years. Biochemists have characterized the constituent proteins and rRNA's of ribosomes. Complete sequences have been determined for some ribosomal proteins and specific antibodies have been prepared against all E. coli small subunit proteins. In addition, a number of naturally occuring systems of three dimensional ribosome crystals which are suitable for structural studies have been observed in eukaryotes. Although the crystals are, in general, too small for X-ray diffraction, their size is ideal for electron microscopy.

Study of the Molecular Architecture of Keratin Filaments by Electron Microscopy

1982 ◽  
Vol 40 ◽  
pp. 118-119
Author(s):  
U. Aebi ◽  
P. Rew ◽  
T.-T. Sun
Keyword(s):  
Electron Microscopy ◽  
Structural Organization ◽  
Cell Types ◽  
Structural Features ◽  
Molecular Architecture ◽  
The Past ◽  
Keratin Filaments ◽  
Different Types ◽  
10 Nm Filaments ◽  
Different Cell Types

Various types of intermediate-sized (10-nm) filaments have been found and described in many different cell types during the past few years. Despite the differences in the chemical composition among the different types of filaments, they all yield common structural features: they are usually up to several microns long and have a diameter of 7 to 10 nm; there is evidence that they are made of several 2 to 3.5 nm wide protofilaments which are helically wound around each other; the secondary structure of the polypeptides constituting the filaments is rich in ∞-helix. However a detailed description of their structural organization is lacking to date.

Aggregated, Conformationally Changed Fibrinogen Exposes the Stimulating Sites for t-PA-Catalysed Plasminogen Activation

1996 ◽  
Vol 75 (02) ◽  
pp. 326-331 ◽  
Author(s):  
Unni Haddeland ◽  
Knut Sletten ◽  
Anne Bennick ◽  
Willem Nieuwenhuizen ◽  
Frank Brosstad
Keyword(s):  
Conformational Changes ◽  
Gel Permeation Chromatography ◽  
Tissue Type ◽  
Plasminogen Activation ◽  
Chromogenic Substrate ◽  
Type Plasminogen Activator ◽  
Gel Permeation ◽  
Self Association ◽  
Fibrin Monomers ◽  
Stimulation Of

SummaryThe present paper shows that conformationally changed fibrinogen can expose the sites Aα-(148-160) and γ-(312-324) involved in stimulation of the tissue-type plasminogen activator (t-PA)-catalysed plasminogen activation. The exposure of the stimulating sites was determined by ELISA using mABs directed to these sites, and was shown to coincide with stimulation of t-PA-catalysed plasminogen activation as assessed in an assay using a chromogenic substrate for plasmin. Gel permeation chromatography of fibrinogen conformationally changed by heat (46.5° C for 25 min) demonstrated the presence of both aggregated and monomeric fibrinogen. The aggregated fibrinogen, but not the monomeric fibrinogen, had exposed the epitopes Aα-(148-160) and γ-(312-324) involved in t-PA-stimulation. Fibrinogen subjected to heat in the presence of 3 mM of the tetrapeptide GPRP neither aggregates nor exposes the rate-enhancing sites. Thus, aggregation and exposure of t-PA-stimulating sites in fibrinogen seem to be related phenomena, and it is tempting to believe that the exposure of stimulating sites is a consequence of the conformational changes that occur during aggregation, or self-association. Fibrin monomers kept in a monomeric state by a final GPRP concentration of 3 mM do not expose the epitopes Aα-(148-160) and γ-(312-324) involved in t-PA-stimulation, whereas dilution of GPRP to a concentration that is no longer anti-polymerizing, results in exposure of these sites. Consequently, the exposure of t-PA-stimulating sites in fibrin as well is due to the conformational changes that occur during selfassociation.

RIBONUCLEOPROTEIN PARTICLES CONTAINING mRNA and pre-mRNA

1973 ◽  
Vol 74 (Suppl) ◽  
pp. S130-S167 ◽  
Author(s):  
O. P. Samarina ◽  
E. M. Lukanidin ◽  
G. P. Georgiev
Keyword(s):  
Structural Organization ◽  
General Scheme ◽  
Biological Significance ◽  
Mrna Transport ◽  
Ribonucleoprotein Particles ◽  
Mrna Precursor

ABSTRACT This paper is a review of the data concerning the nature, structural organization, properties and biological significance of the particles, containing mRNA and pre-mRNA (precursor of mRNA), i. e., (1) nuclear pre-mRNA-containing particles (2) free cytoplasmic mRNP (ribonucleoproteins), or informosomes (3) polysome-bound mRNP. Some new data on the comparison of nuclear and cytoplasmic particles, the nature of poly A-containing structures, involvement of informofers in Adenovirusspecific RNA transfer are presented. The general scheme of mRNA transport from nucleus to cytoplasm is discussed.

Self-association of insulin. Its pH dependence and effect of plasma

Diabetes ◽  
1987 ◽  
Vol 36 (3) ◽  
pp. 261-264 ◽  
Author(s):  
E. Helmerhorst ◽  
G. B. Stokes
Keyword(s):  
Ph Dependence ◽  
Self Association

Quantitative Conditions and Convergent Operations That Are Compatible With the Universe as a Persistent Generator of Successive Simulations

2016 ◽  
Vol 12 (1) ◽  
pp. 4178-4187
Author(s):  
Michael A Persinger ◽  
Stanley A Koren
Keyword(s):  
Structural Organization ◽  
Total Duration ◽  
Human Cognition ◽  
Intrinsic Properties ◽  
Basic Assumptions ◽  
Electron Orbit ◽  
Quantitative Analyses ◽  
Massive Information ◽  
The Universe

                The capacity for computer-like simulations to be generated by massive information processing from electron-spin potentials supports Bostrom’s hypothesis that matter and human cognition might reflect simulations. Quantitative analyses of the basic assumptions indicate the universe may display properties of a simulation where photons behave as pixels and gravitons control the structural organization. The Lorentz solution for the square of the light and entanglement velocities converges with the duration of a single electron orbit that ultimately defines properties of matter. The approximately one trillion potential states within the same space with respect to the final epoch of the universe indicate that a different simulation, each with intrinsic properties, has been and will be generated as a type of tractrix defined by ±2 to 3 days (total duration 5 to 6 days). It may define the causal limits within a simulation. Because of the intrinsic role of photons as the pixel unit, phenomena within which flux densities are enhanced, such as human cognition (particularly dreaming) and the cerebral regions associated with those functions, create the conditions for entanglement or excess correlations between contiguous simulations. The consistent quantitative convergence of operations indicates potential validity for this approach. The emergent solutions offer alternative explanations for the limits of predictions for multivariate phenomena that could be coupled to more distal simulations.

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