[NMR] Postdoc in biomolecular SSNMR - protein aggregation & protein-lipid interactions
From The DNP-NMR Blog:
Postdoc in biomolecular SSNMR - protein aggregation & protein-lipid interactions
Postdoctoral position in biological MAS ssNMR
The Van der Wel lab is looking for a postdoc candidate with a background in NMR, preferably solid-state NMR, to join our research effort focused on protein aggregation and protein-lipid interactions. More information on our research and recent publications can be found below and on our website at http://www.vanderwellab.org
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News from NMR blogs
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05-19-2017 04:01 AM
[NMR paper] Water Proton NMR-A Tool for Protein Aggregation Characterization.
Water Proton NMR-A Tool for Protein Aggregation Characterization.
Related Articles Water Proton NMR-A Tool for Protein Aggregation Characterization.
Anal Chem. 2017 Apr 25;:
Authors: Taraban MB, DePaz RA, Lobo B, Yu YB
Abstract
Formulation stability is a critical attribute of any protein-based biopharmaceutical drug due to a protein's inherent tendency to aggregate. Advanced analytical techniques currently used for characterization of protein aggregates are prone to a number of limitations, and usually require additional...
[NMR paper] Untangling a Repetitive Amyloid Sequence: Correlating Biofilm-Derived and Segmentally Labeled Curli Fimbriae by Solid-State NMR Spectroscopy.
Untangling a Repetitive Amyloid Sequence: Correlating Biofilm-Derived and Segmentally Labeled Curli Fimbriae by Solid-State NMR Spectroscopy.
Related Articles Untangling a Repetitive Amyloid Sequence: Correlating Biofilm-Derived and Segmentally Labeled Curli Fimbriae by Solid-State NMR Spectroscopy.
Angew Chem Int Ed Engl. 2015 Oct 16;
Authors: Schubeis T, Yuan P, Ahmed M, Nagaraj M, van Rossum BJ, Ritter C
Abstract
Curli are functional bacterial amyloids produced by an intricate biogenesis machinery. Insights into their...
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Journal club
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10-17-2015 03:40 PM
Protein aggregation Curling damage - Nature.com
Protein aggregation Curling damage - Nature.com
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Protein aggregation Curling damage
Nature.com
... misfolded proteins was induced. CsgC could inhibit CsgA amyloid formation in vitro, as detected by far-UV CD spectroscopy and NMR, presumably by stabilizing a preamyloid intermediate of CsgA, as detected by an amyloid conformation-specific antibody.
Read here
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Online News
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02-18-2015 06:15 PM
Journal Highlight: Does aluminium bind to histidine? An NMR investigation of amyloid ?12 and amyloid ?16 fragments
Journal Highlight: Does aluminium bind to histidine? An NMR investigation of amyloid ?12 and amyloid ?16 fragments
http://www.spectroscopynow.com/common/images/thumbnails/13f9ef04f37.jpgIn an NMR study of the N-terminal amyloid peptide fragments A?12 and (A?16), non-histidine residues were found to be involved in aluminium binding.
Read the rest at Spectroscopynow.com
Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach.
Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach.
Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach.
Curr Protein Pept Sci. 2011 Feb 24;
Authors: Orcellet ML, Fernández CO
The misfolding of proteins into a toxic conformation is proposed to be at the molecular foundation of a number of neurodegenerative disorders including Alzheimer's and Parkinson's diseases. Evidence that ?-synuclein amyloidogenesis plays a causative role in the development of Parkinson's disease is furnished by a...