Bacteria disarmer activates fiber formation in Parkinson's protein - HealthCanal.com
Bacteria disarmer activates fiber formation in Parkinson's protein - HealthCanal.com
Bacteria disarmer activates fiber formation in Parkinson's protein HealthCanal.com
Most of the study was carried out by post-doctoral fellows Istvan Horvath, Christoph F. Weise, and Emma Andersson. With the assistance of the KBC platform for nuclear magnetic resonance, NMR, the scientists have been able to study proteins at the ...
Structure of key protein associated with Parkinson's disease determined - Science Codex
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Structure of key protein associated with Parkinson's disease determined
Science Codex
Pochapsky's lab was responsible for examining the protein using nuclear magnetic resonance, a sort of MRI for molecules, housed at the Landsman Research Facility. Alpha-synuclein is found in large quantities in the brain. ...
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Structure of key protein associated with Parkinson's disease determined - Science Codex
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10-24-2011 11:06 PM
Structure of Parkinson's disease protein identified - Brandeis University
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Brandeis University
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Structure of Parkinson's disease protein identified
Brandeis University
Pochapsky's lab was responsible for examining the protein using nuclear magnetic resonance, a sort of MRI for molecules. Alpha-synuclein is found in large quantities in the brain. Its association with Parkinson's disease has stirred curiosity since it ...
Structure of Parkinson's disease protein identified - Brandeis University
nmrlearner
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10-21-2011 10:04 PM
[NMR paper] Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the
Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the acetylation of ubiquitin.
Related Articles Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the acetylation of ubiquitin.
J Biol Chem. 2000 Oct 13;275(41):31908-13
Authors: Macdonald JM, Haas AL, London RE
Reactivity of surface lysyl residues of proteins with a broad range of chemical agents has been proposed to be dependent on the catalytic microenvironment of the residue. We have investigated the acetylation of wild type...
nmrlearner
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11-19-2010 08:29 PM
More than a third of our proteins are still a mystery for scientists - HealthCanal.co
More than a third of our proteins are still a mystery for scientists - HealthCanal.com
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More than a third of our proteins are still a mystery for scientists
HealthCanal.com
Several tools to study the structure of these proteins are already available, such as Nuclear Magnetic Resonance and Small-angle X-ray Scattering (SAXS); ...
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nmrlearner
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10-02-2010 12:16 AM
[NMR paper] Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxi
Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin.
Related Articles Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin.
J Biomol NMR. 1994 May;4(3):411-32
Authors: Chandrasekhar K, Campbell AP, Jeng MF, Holmgren A, Dyson HJ
As a prelude to complete structure calculations of both the oxidized and reduced forms of Escherichia coli thioredoxin (M(r) 11,700), we have analyzed the NMR...
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08-22-2010 03:33 AM
[NMR paper] Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxi
Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin.
Related Articles Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin.
J Biomol NMR. 1994 May;4(3):411-32
Authors: Chandrasekhar K, Campbell AP, Jeng MF, Holmgren A, Dyson HJ
As a prelude to complete structure calculations of both the oxidized and reduced forms of Escherichia coli thioredoxin (M(r) 11,700), we have analyzed the NMR...
nmrlearner
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08-22-2010 03:33 AM
[NMR paper] Diffusional limitations of immobilized Escherichia coli in hollow-fiber reactors: inf
Diffusional limitations of immobilized Escherichia coli in hollow-fiber reactors: influence on 31P NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Diffusional limitations of immobilized Escherichia coli in hollow-fiber reactors: influence on 31P NMR spectroscopy.
Biotechnol Bioeng. 1990 Nov;36(9):887-901
Authors: Briasco CA, Karel SF, Robertson CR
Escherichia coli cells were immobilized and grown in hollow-fiber...
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08-21-2010 11:04 PM
[NMR paper] The formation of protein complexes between ferricytochrome b5 and ferricytochrome c s
The formation of protein complexes between ferricytochrome b5 and ferricytochrome c studied using high-resolution 1H-NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles The formation of protein complexes between ferricytochrome b5 and ferricytochrome c studied using high-resolution 1H-NMR spectroscopy.
Eur J Biochem. 1990 Sep 24;192(3):715-21
Authors: Whitford D, Concar DW, Veitch NC, Williams RJ
The association of...