Quantification of secondary and tertiary structure base pairs in E. coli tRNA1Val

Nature ◽  
1976 ◽  
Vol 262 (5567) ◽  
pp. 423-424 ◽  
Author(s):  
PHILIP H. BOLTON ◽  
DAVID R. KEARNS
Keyword(s):  
Tertiary Structure ◽  
Base Pairs ◽  
E Coli ◽  
Secondary And Tertiary Structure

Quantitative determination of the number of secondary and tertiary structure base pairs in transfer RNA in solution

Biochemistry ◽  
1976 ◽  
Vol 15 (20) ◽  
pp. 4370-4377 ◽  
Author(s):  
P. H. Bolton ◽  
C. R. Jones ◽  
D. Bastedo-Lerner ◽  
K. L. Wong ◽  
D. R. Kearns
Keyword(s):  
Quantitative Determination ◽  
Tertiary Structure ◽  
Transfer Rna ◽  
Base Pairs ◽  
Secondary And Tertiary Structure

NMR evidence for common tertiary structure base pairs in yeast and E. coli tRNA

Nature ◽  
1975 ◽  
Vol 255 (5506) ◽  
pp. 347-349 ◽  
Author(s):  
PHILIP H. BOLTON ◽  
DAVID R. KEARNS
Keyword(s):  
Tertiary Structure ◽  
Base Pairs ◽  
E Coli

Secondary and tertiary structure prediction of fenugreek (Trigonella foenum-graecum) protein

2016 ◽  
Vol 39 (1) ◽  
Author(s):  
Sharda Choudhary ◽  
Ravindra Singh ◽  
R. S. Meena ◽  
Geetika Jethra
Keyword(s):  
Structure Prediction ◽  
Tertiary Structure ◽  
Transmembrane Protein ◽  
Protein Domain ◽  
E Coli ◽  
Trigonella Foenum Graecum ◽  
Lab Experiments ◽  
Wet Lab ◽  
Protein Models ◽  
Secondary And Tertiary Structure

<italic>In-silico</italic> development of protein models in fenugreek (<italic>Trigonella foenum-graecum</italic>) has opened up new vistas using the modern computational tools. The identification of protein in fenugreek having homology with the protein domain of humans and E-coli shows that the database available on Apiaceae family are very low. The estimated molecular weight of identified for fenugreek AM-1 protein was 11372.8 and was predicted as basic. A channel in fenugreek transmembrane protein has been identified through which a ligand (an ion or a small molecule) might pass. The present finding may be a valuable addition to the proteomic information available on fenugreek. Further validation can be performed using wet lab experiments.

scholarly journals Characterization of the type I dehydroquinase from Salmonella typhi

1993 ◽  
Vol 295 (1) ◽  
pp. 277-285 ◽  
Author(s):  
J D Moore ◽  
A R Hawkins ◽  
I G Charles ◽  
R Deka ◽  
J R Coggins ◽  
...  
Keyword(s):  
Tertiary Structure ◽  
Salmonella Typhi ◽  
Type I ◽  
Active Site Residues ◽  
X Ray ◽  
E Coli ◽  
Product Mixture ◽  
Secondary And Tertiary Structure ◽  
Nabh4 Reduction

The type I dehydroquinase from the human pathogen Salmonella typhi was overexpressed in an Escherichia coli host and purified to homogeneity. The S. typhi enzyme was characterized in terms of its kinetic parameters, important active-site residues, thermal stability and c.d. and fluorescence properties. In all important respects, the enzyme from S. typhi behaves in a very similar fashion to the well-characterized enzyme from E. coli, including the remarkable conformational stabilization observed on reduction of the substrate/product mixture by NaBH4. This gives confidence that the information from X-ray studies on the S. typhi enzyme [Boys, Fawcett, Sawyer, Moore, Charles, Hawkins, Deka, Kleanthous and Coggins (1992) J. Mol. Biol. 227, 352-355] can be applied to other type I dehydroquinases. Studies of the quenching of fluorescence of the S. typhi enzyme by succinimide show that NaBH4 reduction of the substrate/product imine complex involves a dramatic decrease in the flexibility of the enzyme, with only very minor changes in the overall secondary and tertiary structure.

Production of recombinant porin from Y. pseudotuberculosis in a water-soluble form for pseudotuberculosis diagnostics

2017 ◽  
Vol 398 (11) ◽  
pp. 1229-1236 ◽  
Author(s):  
Vasily Golotin ◽  
Olga Portnyagina ◽  
Natalia Chopenko ◽  
Natalia Kim ◽  
Valery Rasskazov ◽  
...  
Keyword(s):  
Recombinant Protein ◽  
Spatial Structure ◽  
Outer Membrane ◽  
Yersinia Pseudotuberculosis ◽  
Tertiary Structure ◽  
Water Soluble ◽  
Soluble Form ◽  
E Coli ◽  
Diagnostic Antigen ◽  
Secondary And Tertiary Structure

AbstractOmpF porin from the outer membrane ofYersinia pseudotuberculosiswas cloned into pET-40b(+) plasmid. UsingE. coliRosetta (DE3) strain, MX medium, IPTG concentration of 0.2 mmand post-induction cultivation at 14°C overnight allowed us to obtain a water-soluble form of the recombinant protein (rs-OmpF). Rs-OmpF was shown to have the ordered spatial structure at the levels of secondary and tertiary structure. Rs-OmpF was found to be effective as diagnostic antigen in ELISA for pseudotuberculosis diagnostics.

Developing a Genetic System in Deinococcus radiodurans for Analyzing Mutations

Genetics ◽  
2004 ◽  
Vol 166 (2) ◽  
pp. 661-668
Author(s):  
Mandy Kim ◽  
Erika Wolff ◽  
Tiffany Huang ◽  
Lilit Garibyan ◽  
Ashlee M Earl ◽  
...  
Keyword(s):  
Dna Sequences ◽  
Deinococcus Radiodurans ◽  
Genetic System ◽  
Base Change ◽  
Base Substitution ◽  
Wild Type ◽  
Base Pairs ◽  
E Coli ◽  
Radiation Induced ◽  
Induced Mutagenesis

Abstract We have applied a genetic system for analyzing mutations in Escherichia coli to Deinococcus radiodurans, an extremeophile with an astonishingly high resistance to UV- and ionizing-radiation-induced mutagenesis. Taking advantage of the conservation of the β-subunit of RNA polymerase among most prokaryotes, we derived again in D. radiodurans the rpoB/Rif r system that we developed in E. coli to monitor base substitutions, defining 33 base change substitutions at 22 different base pairs. We sequenced &gt;250 mutations leading to Rif r in D. radiodurans derived spontaneously in wild-type and uvrD (mismatch-repair-deficient) backgrounds and after treatment with N-methyl-N′-nitro-N-nitrosoguanidine (NTG) and 5-azacytidine (5AZ). The specificities of NTG and 5AZ in D. radiodurans are the same as those found for E. coli and other organisms. There are prominent base substitution hotspots in rpoB in both D. radiodurans and E. coli. In several cases these are at different points in each organism, even though the DNA sequences surrounding the hotspots and their corresponding sites are very similar in both D. radiodurans and E. coli. In one case the hotspots occur at the same site in both organisms.

scholarly journals Soluble Expression and Efficient Purification of Recombinant Class I Hydrophobin DewA

2021 ◽  
Vol 22 (15) ◽  
pp. 7843
Author(s):  
Sang-Oh Ahn ◽  
Ho-Dong Lim ◽  
Sung-Hwan You ◽  
Dae-Eun Cheong ◽  
Geun-Joong Kim
Keyword(s):  
Tertiary Structure ◽  
Signal Sequence ◽  
Soluble Expression ◽  
Class I ◽  
Soluble Form ◽  
Two Phase ◽  
E Coli ◽  
Small Proteins ◽  
Industrial Use ◽  
Shed Light

Hydrophobins are small proteins (<20 kDa) with an amphipathic tertiary structure that are secreted by various filamentous fungi. Their amphipathic properties provide surfactant-like activity, leading to the formation of robust amphipathic layers at hydrophilic–hydrophobic interfaces, which make them useful for a wide variety of industrial fields spanning protein immobilization to surface functionalization. However, the industrial use of recombinant hydrophobins has been hampered due to low yield from inclusion bodies owing to the complicated process, including an auxiliary refolding step. Herein, we report the soluble expression of a recombinant class I hydrophobin DewA originating from Aspergillus nidulans, and its efficient purification from recombinant Escherichia coli. Soluble expression of the recombinant hydrophobin DewA was achieved by a tagging strategy using a systematically designed expression tag (ramp tag) that was fused to the N-terminus of DewA lacking the innate signal sequence. Highly expressed recombinant hydrophobin DewA in a soluble form was efficiently purified by a modified aqueous two-phase separation technique using isopropyl alcohol. Our approach for expression and purification of the recombinant hydrophobin DewA in E. coli shed light on the industrial production of hydrophobins from prokaryotic hosts.

scholarly journals THE DNA OF CAENORHABDITIS ELEGANS

Genetics ◽  
1974 ◽  
Vol 77 (1) ◽  
pp. 95-104
Author(s):  
J E Sulston ◽  
S Brenner
Keyword(s):  
Caenorhabditis Elegans ◽  
Chemical Analysis ◽  
Dna Sequences ◽  
Base Composition ◽  
Nematode Caenorhabditis Elegans ◽  
5S Rna ◽  
Base Pairs ◽  
Small Component ◽  
E Coli ◽  
The Mean

ABSTRACT Chemical analysis and a study of renaturation kinetics show that the nematode, Caenorhabditis elegans, has a haploid DNA content of 8 x IO7 base pairs (20 times the genome of E. coli). Eighty-three percent of the DNA sequences are unique. The mean base composition is 36% GC; a small component, containing the rRNA cistrons, has a base composition of 51% GC. The haploid genome contains about 300 genes for 4s RNA, 110 for 5s RNA, and 55 for (18 + 28)S RNA.

Sign in / Sign up

Export Citation Format

Share Document