scholarly journals Redesign of a Copper Storage Protein into an Artificial Hydrogenase

ACS Catalysis ◽  
2019 ◽  
Vol 9 (7) ◽  
pp. 5847-5859 ◽  
Author(s):  
Dhanashree Selvan ◽  
Pallavi Prasad ◽  
Erik R. Farquhar ◽  
Yelu Shi ◽  
Skyler Crane ◽  
...  
Keyword(s):  
Storage Protein ◽  
Copper Storage

scholarly journals The oxygen reactivity of an artificial hydrogenase designed in a reengineered copper storage protein

2020 ◽  
Vol 49 (6) ◽  
pp. 1928-1934
Author(s):  
Dhanashree Selvan ◽  
Yelu Shi ◽  
Pallavi Prasad ◽  
Skyler Crane ◽  
Yong Zhang ◽  
...  
Keyword(s):  
Storage Protein ◽  
Binding Protein ◽  
Nickel Binding ◽  
Copper Storage ◽  
Oxygen Reactivity

The O2 reactivity of an artificial biomolecular hydrogenase, the nickel binding protein (NBP) is investigated.

Intrinsically fluorescent gold nanoclusters stabilized within a copper storage protein that follow the Irving–Williams trend in metal ion sensing

The Analyst ◽  
2019 ◽  
Vol 144 (13) ◽  
pp. 3949-3958 ◽  
Author(s):  
Dhanashree Selvan ◽  
Pallavi Prasad ◽  
Skyler Crane ◽  
Abubkr Abuhagr ◽  
Richard Covington ◽  
...  
Keyword(s):  
Storage Protein ◽  
Metal Ion ◽  
Gold Nanoclusters ◽  
Gold Clusters ◽  
Ion Sensing ◽  
Metal Detection ◽  
Metal Ion Sensing ◽  
Copper Storage ◽  
Tunable Emission

A copper storage protein is used to synthesize gold clusters with tunable emission that follow the Irving–Williams series for metal detection.

scholarly journals A cytosolic copper storage protein provides a second level of copper tolerance inStreptomyces lividans

Metallomics ◽  
2018 ◽  
Vol 10 (1) ◽  
pp. 180-193 ◽  
Author(s):  
Megan L. Straw ◽  
Amanda K. Chaplin ◽  
Michael A. Hough ◽  
Jordi Paps ◽  
Vassiliy N. Bavro ◽  
...  
Keyword(s):  
Storage Protein ◽  
Streptomyces Lividans ◽  
Copper Resistance ◽  
Copper Tolerance ◽  
Copper Storage

A cytosolic copper storage protein has been identified inStreptomyces lividansand plays a role in copper tolerance once the first layer of copper resistance becomes saturated.

Where is the prolamine located in rice endosperm?

1990 ◽  
Vol 48 (3) ◽  
pp. 696-697
Author(s):  
Hsin-Kan Wu ◽  
Mei-Chu Chung
Keyword(s):  
Storage Protein ◽  
Sodium Phosphate ◽  
Recent Experiment ◽  
Protein A ◽  
Uranyl Acetate ◽  
Protein Bodies ◽  
Lead Citrate ◽  
Thin Sections ◽  
Rice Endosperm ◽  
Ethanol Series

In one of our earlier papers (Wu et al. 1978), we suggested that glutelin is the major composition of the round storage protein bodies although they also contain relatively more prolamine than the angular one does. Immunochemical studies of Krishnan et al. (1986) later showed the presence of glutelin in the irregularly-shaped (angular) protein bodies while the prolamines were found in the round ones. Our recent experiment using protein A-gold technique found that prolamine is mainly deposited into the angular protein bodies.Small blocks (1 mm3) of 7 DAF (days after flowering) caryopsis of Orvza perennis were fixed with 3% paraformaldehyde and 3% glutaraldehyde in 0.1M sodium phosphate, pH7.4, dehydrated in a graded ethanol series and infiltrated with Spurr’s resin. Thin sections, after gold labeling, were stained with uranyl acetate and lead citrate. Rabbit antibodies were raised against purified prolamine. Protein A-gold sol complex was prepared based on the technique of Horisberger et al. (1977).

scholarly journals Molecular cytogenetical and biochemical studies on some Lupinus species

2021 ◽  
Vol 45 (1) ◽  
Author(s):  
Hoda B. M. Ali ◽  
Samy A. A. Heiba
Keyword(s):  
Related Species ◽  
Storage Protein ◽  
Seed Storage Protein ◽  
Lupinus Albus ◽  
Seed Storage ◽  
Rrna Genes ◽  
Large Chromosome ◽  
45S Rdna ◽  
Lupinus Polyphyllus ◽  
Electrophoretic Patterns

Abstract Background Lupins are cultivated as human consumption grains and forage legumes. The chromosomes of lupins are too small to be karyotyped by conventional techniques, because they reveal a general lack of distinctive cytological features. In the current study, Fluorescence in situ Hybridization (FISH) was used to locate 5S and 45S ribosomal gene sites on the chromosomes of Lupinus albus ssp albus, Lupinus albus ssp graecus, Lupnus termis (all with 2n = 50), and Lupinus polyphyllus lindl var. polyphyllus (2n = 48), FISH together with seed storage protein electrophoretic patterns were used to find out the relationship among these species. Results The double-target FISH on the chromosomes of the studied species with rDNA probes revealed that the two types of rRNA genes are located on different chromosomes. The detected loci of rRNA genes partially reflected the taxonomical similarity among the two Lupinus albus subspecies and L. termis. Lupinus polyphyllus lindl var. polyphyllus was exception by having unique large chromosome mostly is covered by one signal of 45S rDNA, whereas its homologous chromosome seems to be normal-sized and have the other 45S rDNA locus. The similarity matrix among the Lupinus species as computed according to Jaccardʼs Coefficient from the SDS-PAGE, showed that L. albus ssp. Albus and L. albus ssp. Graecus are the most similar species (~ 97%), and then comes L. termis, and L. polyphyllus lindl var. polyphylus has been placed in separate clade and still the most related species to it among the studied species is L. termis (~ 70%). Conclusion It could be postulated from FISH and seed storage protein electrophoretic patterns that the relationships among the studied species is as follows, Lupinus albus ssp albus, is the most related species to Lupinus albus ssp graecus then comes Lupnus termis and Lupinus polyphyllus lindl var. polyphyllus at a distal position.

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