scholarly journals Completing the family of human EH domains: Solution structure of the internal EH domain of γ‐synergin

2021 ◽  
Author(s):  
Michael Kovermann ◽  
Ulrich Weininger ◽  
Christian Löw
Keyword(s):  
Solution Structure ◽  
The Family ◽  
Eh Domain

Solution Structure of Eps15's Third EH Domain Reveals Coincident Phe−Trp and Asn−Pro−Phe Binding Sites†,‡

Biochemistry ◽  
2000 ◽  
Vol 39 (15) ◽  
pp. 4309-4319 ◽  
Author(s):  
Jennifer L. Enmon ◽  
Tonny de Beer ◽  
Michael Overduin
Keyword(s):  
Binding Sites ◽  
Solution Structure ◽  
Eh Domain

scholarly journals Solution structure of the cold-shock-like protein fromRickettsia rickettsii

2012 ◽  
Vol 68 (11) ◽  
pp. 1284-1288 ◽  
Author(s):  
Kyle P. Gerarden ◽  
Andrew M. Fuchs ◽  
Jonathan M. Koch ◽  
Melissa M. Mueller ◽  
David R. Graupner ◽  
...  
Keyword(s):  
Solution Structure ◽  
Cold Shock ◽  
Spotted Fever ◽  
Rocky Mountain ◽  
Rocky Mountain Spotted Fever ◽  
Cold Shock Proteins ◽  
Rickettsia Rickettsii ◽  
The Family ◽  
Α Helix ◽  
Shock Proteins

Rocky Mountain spotted fever is caused byRickettsia rickettsiiinfection.R. rickettsiican be transmitted to mammals, including humans, through the bite of an infected hard-bodied tick of the family Ixodidae. Since theR. rickettsiigenome contains only one cold-shock-like protein and given the essential nature of cold-shock proteins in other bacteria, the structure of the cold-shock-like protein fromR. rickettsiiwas investigated. With the exception of a short α-helix found between β-strands 3 and 4, the solution structure of theR. rickettsiicold-shock-like protein has the typical Greek-key five-stranded β-barrel structure found in most cold-shock domains. Additionally, theR. rickettsiicold-shock-like protein, with a ΔGof unfolding of 18.4 kJ mol−1, has a similar stability when compared with other bacterial cold-shock proteins.

Solution Structure of the Reps1 EH Domain and Characterization of Its Binding to NPF Target Sequences†,‡

Biochemistry ◽  
2001 ◽  
Vol 40 (23) ◽  
pp. 6776-6785 ◽  
Author(s):  
Soyoun Kim ◽  
Donald N. Cullis ◽  
Larry A. Feig ◽  
James D. Baleja
Keyword(s):  
Solution Structure ◽  
Eh Domain ◽  
Target Sequences

Triassic sponges (Sphinctozoa) from Hells Canyon, Oregon

1988 ◽  
Vol 62 (03) ◽  
pp. 419-423 ◽  
Author(s):  
Baba Senowbari-Daryan ◽  
George D. Stanley
Keyword(s):  
Endemic Species ◽  
Upper Triassic ◽  
Island Arc ◽  
Tropical Island ◽  
The Family ◽  
Wallowa Terrane ◽  
Unique Condition ◽  
Hells Canyon

Two Upper Triassic sphinctozoan sponges of the family Sebargasiidae were recovered from silicified residues collected in Hells Canyon, Oregon. These sponges areAmblysiphonellacf.A. steinmanni(Haas), known from the Tethys region, andColospongia whalenin. sp., an endemic species. The latter sponge was placed in the superfamily Porata by Seilacher (1962). The presence of well-preserved cribrate plates in this sponge, in addition to pores of the chamber walls, is a unique condition never before reported in any porate sphinctozoans. Aporate counterparts known primarily from the Triassic Alps have similar cribrate plates but lack the pores in the chamber walls. The sponges from Hells Canyon are associated with abundant bivalves and corals of marked Tethyan affinities and come from a displaced terrane known as the Wallowa Terrane. It was a tropical island arc, suspected to have paleogeographic relationships with Wrangellia; however, these sponges have not yet been found in any other Cordilleran terrane.

Electron Microscopy of Mycoplasma Pneumoniae

1971 ◽  
Vol 29 ◽  
pp. 258-259 ◽  
Author(s):  
E. S. Boatman ◽  
G. E. Kenny
Keyword(s):  
Electron Microscopy ◽  
Light Microscopy ◽  
Growth Phase ◽  
Hela Cells ◽  
Sulfonic Acid ◽  
Gamma Globulin ◽  
Horse Serum ◽  
Morphological Aspects ◽  
The Family

Information concerning the morphology and replication of organism of the family Mycoplasmataceae remains, despite over 70 years of study, highly controversial. Due to their small size observations by light microscopy have not been rewarding. Furthermore, not only are these organisms extremely pleomorphic but their morphology also changes according to growth phase. This study deals with the morphological aspects of M. pneumoniae strain 3546 in relation to growth, interaction with HeLa cells and possible mechanisms of replication.The organisms were grown aerobically at 37°C in a soy peptone yeast dialysate medium supplemented with 12% gamma-globulin free horse serum. The medium was buffered at pH 7.3 with TES [N-tris (hyroxymethyl) methyl-2-aminoethane sulfonic acid] at 10mM concentration. The inoculum, an actively growing culture, was filtered through a 0.5 μm polycarbonate “nuclepore” filter to prevent transfer of all but the smallest aggregates. Growth was assessed at specific periods by colony counts and 800 ml samples of organisms were fixed in situ with 2.5% glutaraldehyde for 3 hrs. at 4°C. Washed cells for sectioning were post-fixed in 0.8% OSO4 in veronal-acetate buffer pH 6.1 for 1 hr. at 21°C. HeLa cells were infected with a filtered inoculum of M. pneumoniae and incubated for 9 days in Leighton tubes with coverslips. The cells were then removed and processed for electron microscopy.

Exposure of protein VP7 on the surface of bluetongue virus

1990 ◽  
Vol 48 (3) ◽  
pp. 600-601
Author(s):  
A.D. Hyatt
Keyword(s):  
Bluetongue Virus ◽  
Structural Proteins ◽  
Major Constituent ◽  
Outer Coat ◽  
Virus Particles ◽  
Antibody Recognition ◽  
The Core ◽  
The Family ◽  
Electron Microscopical ◽  
Physical Accessibility

Bluetongue virus (BTV) is the type species os the genus orbivirus in the family Reoviridae. The virus has a fibrillar outer coat containing two major structural proteins VP2 and VP5 which surround an icosahedral core. The core contains two major proteins VP3 and VP7 and three minor proteins VP1, VP4 and VP6. Recent evidence has indicated that the core comprises a neucleoprotein center which is surrounded by two protein layers; VP7, a major constituent of capsomeres comprises the outer and VP3 the inner layer of the core . Antibodies to VP7 are currently used in enzyme-linked immunosorbant assays and immuno-electron microscopical (JEM) tests for the detection of BTV. The tests involve the antibody recognition of VP7 on virus particles. In an attempt to understand how complete viruses can interact with antibodies to VP7 various antibody types and methodologies were utilized to determine the physical accessibility of the core to the external environment.

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