[NMR paper] In*vitro mutagenicity, NMR metabolite characterization of azo and triphenylmethanes dyes by adherents bacteria and the role of the "cna" adhesion gene in activated sludge.
In*vitro mutagenicity, NMR metabolite characterization of azo and triphenylmethanes dyes by adherents bacteria and the role of the "cna" adhesion gene in activated sludge.
Related ArticlesIn*vitro mutagenicity, NMR metabolite characterization of azo and triphenylmethanes dyes by adherents bacteria and the role of the "cna" adhesion gene in activated sludge.
Microb Pathog. 2017 Feb;103:29-39
Authors: Ayed L, Bakir K, Ben Mansour H, Hammami S, Cheref A, Bakhrouf A
Abstract
Staphylococcus aureus, showing the greatest decolorization ability, was further investigated for Methyl Red (MR) Congo Red (CR), Crystal Violet (CV) and Malachite Green (MG) decolorization using response surface methodology (RSM). The chemometric methods use, based on statistical design of experiments (DOEs) such as RSM is becoming increasingly widespread in several sciences such as analytical chemistry, engineering and environmental chemistry. Stapphylococcus aureus ATCC 25923, Stapphylococcus aureus (S1) and Stapphylococcus aureus (S2), were isolated from textile wastewater plant located in KsarHellal, Tunisia and were tested for their decolorization capacity. PCR technique was utilized to identify the 3 bacterial strains and to detect the adhesin gene "cna". Biodegradation of MR, CR, CV and MG (750*ppm), were investigated under shaking condition in Mineral Salt Medium (MSM) solution at pH 7.5 and temperature 30*°C, using a 3.7*×*10(5)*CFU/ml as inoculum size. Our results showed that Staphylococcus aureus had a high decolorization capacity. Nuclear magnetic resonance (NMR) spectroscopy analysis confirmed the biodegradation of dyes. The four dyes mutagenicity with the S9 metabolizing system decreased significantly after biodegradation and totally disappeared. Nuclear magnetic resonance (NMR) spectroscopy analysis confirmed the biodegradation of dyes.
Petition to "Reclaim the Magnetic Resonance Gordon Research Conference"
Petition to "Reclaim the Magnetic Resonance Gordon Research Conference"
Dear Colleagues,
Please see the link below regarding a petition to start a new Gordon Research Conference on "Frontiers of Magnetic Resonance". The short version is that the original Magnetic Resonance GRC was unfortunately cancelled recently due to insufficient attendance over the past several years, perceived by the GRC organizers to be due to the lack of interest in the magnetic resonance community - much more information on this is provided in the link below.
...
nmrlearner
Conferences
0
07-17-2012 07:38 PM
NMR Characterization of a "Fibril-Ready" State of Demetalated Wild-Type Superoxide Dismutase.
NMR Characterization of a "Fibril-Ready" State of Demetalated Wild-Type Superoxide Dismutase.
NMR Characterization of a "Fibril-Ready" State of Demetalated Wild-Type Superoxide Dismutase.
J Am Chem Soc. 2010 Dec 16;
Authors: Banci L, Bertini I, Blaževitš O, Cantini F, Lelli M, Luchinat C, Mao J, Vieru M
Demetalated superoxide dismutase (SOD1) is a transient species, fibrillogenic in nature and of biomedical interest. It is a conformationally disordered protein difficult to characterize. We have developed a strategy based on the NMR investigation...
Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholi
Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholipid Bilayers Give Equivalent Angular Constraints for NMR Structure Determination.
Related Articles Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholipid Bilayers Give Equivalent Angular Constraints for NMR Structure Determination.
J Phys Chem B. 2010 Oct 20;
Authors: Park SH, Das BB, De Angelis AA, Scrima M, Opella SJ
The native environment for membrane proteins is the highly asymmetric phospholipid bilayer, and this has a large...
[NMR paper] NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease.
NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease.
J Mol Biol. 1995 Jul 7;250(2):134-43
Authors: Alexandrescu AT, Gittis AG, Abeygunawardana C, Shortle D
Similar folds often occur in proteins with dissimilar sequences. The OB-fold forms a part of the structures of at least seven non-homologous proteins...
nmrlearner
Journal club
0
08-22-2010 03:50 AM
Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York
Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York
A postdoctoral position to study the solution dynamics and structure
of protein kinases is available on a NIH funded project (REF#:
HS-R-6453-10-08-S). Our group is interested in how static and dynamic
changes of protein structure affect the activity of protein kinases.
We combine X-ray crystallography, NMR and ligand binding kinetics with
collaborative molecular dynamic studies (See e.g. ref 1 and 2). Our
research group is located at Stony Brook University in a highly
interactive environment with the New York...
In*vitro mutagenicity, NMR metabolite characterization of azo and triphenylmethanes dyes by adherents bacteria and the role of the "cna" adhesion gene in activated sludge.
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