Optimization of overexpression of a chaperone protein of steroid C25 dehydrogenase for biochemical and biophysical characterization

doi:10.1016/j.pep.2017.03.019

Title: Optimization of overexpression of a chaperone protein of steroid C25 dehydrogenase for biochemical and biophysical characterization

Full Record
Other Related Research

Authors:

Niedzialkowska, Ewa; Mrugała, Beata; Rugor, Agnieszka;

; Skotnicka, Anna; Cotelesage, Julien J. H.; George, Graham N.; Szaleniec, Maciej;

; Lewiński, Krzysztof

Publication Date:: 2017-06-01

Sponsoring Org.:: USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)

OSTI Identifier:: 1416244

Resource Type:: Publisher's Accepted Manuscript

Journal Name:: Protein Expression and Purification

Additional Journal Information:: Journal Name: Protein Expression and Purification Journal Volume: 134 Journal Issue: C; Journal ID: ISSN 1046-5928

Publisher:: Elsevier

Country of Publication:: United States

Language:: English

Citation Formats


                    Niedzialkowska, Ewa, Mrugała, Beata, Rugor, Agnieszka, Czub, Mateusz P., Skotnicka, Anna, Cotelesage, Julien J. H., George, Graham N., Szaleniec, Maciej, Minor, Wladek, and Lewiński, Krzysztof. Optimization of overexpression of a chaperone protein of steroid C25 dehydrogenase for biochemical and biophysical characterization.  United States: N. p., 2017. 
        Web.  doi:10.1016/j.pep.2017.03.019.

Copy to clipboard


                    Niedzialkowska, Ewa, Mrugała, Beata, Rugor, Agnieszka, Czub, Mateusz P., Skotnicka, Anna, Cotelesage, Julien J. H., George, Graham N., Szaleniec, Maciej, Minor, Wladek, & Lewiński, Krzysztof. Optimization of overexpression of a chaperone protein of steroid C25 dehydrogenase for biochemical and biophysical characterization.  United States.  doi:10.1016/j.pep.2017.03.019.

Copy to clipboard


                    Niedzialkowska, Ewa, Mrugała, Beata, Rugor, Agnieszka, Czub, Mateusz P., Skotnicka, Anna, Cotelesage, Julien J. H., George, Graham N., Szaleniec, Maciej, Minor, Wladek, and Lewiński, Krzysztof. Thu .  
        "Optimization of overexpression of a chaperone protein of steroid C25 dehydrogenase for biochemical and biophysical characterization".  United States.  doi:10.1016/j.pep.2017.03.019.

Copy to clipboard


                    
@article{osti_1416244,

  title        = {Optimization of overexpression of a chaperone protein of steroid C25 dehydrogenase for biochemical and biophysical characterization},

  author       = {Niedzialkowska, Ewa and Mrugała, Beata and Rugor, Agnieszka and Czub, Mateusz P. and Skotnicka, Anna and Cotelesage, Julien J. H. and George, Graham N. and Szaleniec, Maciej and Minor, Wladek and Lewiński, Krzysztof},

  abstractNote = {},

  doi          = {10.1016/j.pep.2017.03.019},

  journal      = {Protein Expression and Purification},

  number       = C,

  volume       = 134,

  place        = {United States},

  year         = {2017},

  month        = {6}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Accepted Manuscript (Publisher)

Publisher's Version of Record
DOI: 10.1016/j.pep.2017.03.019

Other availability

Search WorldCat to find libraries that may hold this journal

Citation Metrics:

Cited by: 4 works

Citation information provided by
Web of Science

Save / Share:

Export Metadata

Save to My Library

Similar Records in DOE PAGES and OSTI.GOV collections:

Structural and Biophysical Characterization of the Mycobacterium tuberculosis Protein Rv0577, a Protein Associated with Neutral Red Staining of Virulent Tuberculosis Strains and Homologue of the Streptomyces coelicolor Protein KbpA [Structural and Biophysical Characterization of Rv0577, a Protein Associated with Neutral Red Staining of Virulent Strains of Mycobacterium tuberculosis and homolog of the Streptomyces coelicolor protein KbpA]

Journal Article Buchko, Garry W. ; Echols, Nathaniel ; Flynn, E. Megan ; ... - Biochemistry

Mycobacterium tuberculosis protein Rv0577 is a prominent antigen in tuberculosis patients, the component responsible for neutral red staining of virulent strains of M. tuberculosis, a putative component in a methylglyoxal detoxification pathway, and an agonist of toll-like receptor 2. It also has an amino acid sequence that is 36% identical to that of Streptomyces coelicolor AfsK-binding protein A (KbpA), a component in the complex secondary metabolite pathways in the Streptomyces genus. To gain insight into the biological function of Rv0577 and the family of KpbA kinase regulators, the crystal structure for Rv0577 was determined to a resolution of 1.75 Å,more »« less
DOI: 10.1021/acs.biochem.7b00511

Full Text Available
Toxoplasma gondii: Biochemical and biophysical characterization of recombinant soluble dense granule proteins GRA2 and GRA6

Journal Article Bittame, Amina ; Université Grenoble Alpes, 38042 Grenoble ; Effantin, Grégory ; ... - Biochemical and Biophysical Research Communications

The most prominent structural feature of the parasitophorous vacuole (PV) in which the intracellular parasite Toxoplasma gondii proliferates is a membranous nanotubular network (MNN), which interconnects the parasites and the PV membrane. The MNN function remains unclear. The GRA2 and GRA6 proteins secreted from the parasite dense granules into the PV have been implicated in the MNN biogenesis. Amphipathic alpha-helices (AAHs) predicted in GRA2 and an alpha-helical hydrophobic domain predicted in GRA6 have been proposed to be responsible for their membrane association, thereby potentially molding the MMN in its structure. Here we report an analysis of the recombinant proteins (expressedmore »« less
DOI: 10.1016/J.BBRC.2015.02.078
Biochemical and biophysical characterization of the major outer surface protein, OSP-A from North American and European isolates of Borrelia burgdorferi

Conference McGrath, B C ; Dunn, J J ; France, L L ; ...

Lyme borreliosis, caused by the spirochete Borrelia burgdorferi, is the most common vector-borne disease in North America and Western Europe. As the major delayed immune response in humans, a better understanding of the major outer surface lipoproteins OspA and OspB are of much interest. These proteins have been shown to exhibit three distinct phylogenetic genotypes based on their DNA sequences. This paper describes the cloning of genomic DNA for each variant and amplification of PCR. DNA sequence data was used to derive computer driven phylogenetic analysis and deduced amino acid sequences. Overproduction of variant OspAs was carried out in E.more »« less
Full Text Available
Biochemical, biophysical, and molecular genetic studies on the membrane-bound D-lactate dehydrogenase from Escherichia coli

Thesis/Dissertation Rule, G S

The membrane-bound D-lactate dehydrogenase (D-LDH) from E. coli has been used as a model system in order to study structure-function relationships in membrane proteins. This enzyme is activated by various lipids and detergents in vitro, and appears to provide energy for the active transport of amino acids and sugars in E. coli membrane vesicles. In order to obtain sufficient amounts of enzyme for /sup 19/F nuclear magnetic resonance (NMR) and circular dichroism (CD) experiments, the cloned dld gene was used to construct a plasmid in which the expression of D-LDH is induced by a temperature shift. Upon temperature induction, themore »« less
Biochemical and Physiological Characterization: Development & Apply Optical Methods for Charaterizing Biochemical Protein-Protein Interactions in MR-1

Technical Report Weiss, Shimon

The objectives of this report are to: Develop novel site-specific protein labeling chemistries for assaying protein-protein interactions in MR-1; and development of a novel optical acquisition and data analysis method for characterizing protein-protein interactions in MR-1 model systems. Our work on analyzing protein-protein interactions in MR-1 is divided in four areas: (1) expression and labeling of MR-1 proteins; (2) general scheme for site-specific fluorescent labeling of expressed proteins; (3) methodology development for monitoring protein-protein interactions; and (4) study of protein-protein interactions in MR-1. In this final report, we give an account for our advances in all areas.
DOI: 10.2172/890585

Full Text Available

Similar Records