The effects of two macromolecular cosolutes, specifically the polysaccharide dextran-20 and the protein lysozyme, on the aggregation kinetics of a pathogenic huntingtin exon-1 protein (hht^(ex1)) with a 35 polyglutamine repeat, htt^(ex1)Q(35), are described. A unified kinetic model that establishes a direct connection between reversible tetramerization occurring on the microsecond time scale and irreversible fibril formation on a time scale of hours/days forms the basis for quantitative analysis...
[NMR paper] Amyloid fibril formation kinetics of low-pH denatured bovine PI3K-SH3 monitored by three different NMR techniques
Amyloid fibril formation kinetics of low-pH denatured bovine PI3K-SH3 monitored by three different NMR techniques
Introduction: Misfolding of amyloidogenic proteins is a molecular hallmark of neurodegenerative diseases in humans. A detailed understanding of the underlying molecular mechanisms is mandatory for developing innovative therapeutic approaches. The bovine PI3K-SH3 domain has been a model system for aggregation and fibril formation. Methods: We monitored the fibril formation kinetics of low pH-denatured recombinantly expressed labeled bovine PI3K-SH3 by a combination of...
[NMR paper] Quantitative NMR analysis of the kinetics of prenucleation oligomerization and aggregation of pathogenic huntingtin exon-1 protein
Quantitative NMR analysis of the kinetics of prenucleation oligomerization and aggregation of pathogenic huntingtin exon-1 protein
The N-terminal region of the huntingtin protein, encoded by exon-1 (htt^(ex1)) and containing an expanded polyglutamine tract, forms fibrils that accumulate in neuronal inclusion bodies, resulting in Huntington's disease. We previously showed that reversible formation of a sparsely populated tetramer of the N-terminal amphiphilic domain, comprising a dimer of dimers in a four-helix bundle configuration, occurs on the microsecond timescale and is an essential...
[NMR paper] Effects of Excipients on the Structure and Dynamics of Filgrastim Monitored by Thermal Unfolding Studies by CD and NMR Spectroscopy.
Effects of Excipients on the Structure and Dynamics of Filgrastim Monitored by Thermal Unfolding Studies by CD and NMR Spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.png Related Articles Effects of Excipients on the Structure and Dynamics of Filgrastim Monitored by Thermal Unfolding Studies by CD and NMR Spectroscopy.
ACS Omega. 2020 Dec 15;5(49):31845-31857
Authors: Ghasriani H, Frahm GE, Johnston MJW, Aubin Y
Abstract
Product excipients...
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12-29-2020 04:50 AM
Disordered Nanostructure in Huntingtin InteractingProtein K Acts as a Stabilizing Switch To Prevent Protein Aggregation
Disordered Nanostructure in Huntingtin InteractingProtein K Acts as a Stabilizing Switch To Prevent Protein Aggregation
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00776/20180213/images/medium/bi-2017-00776d_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00776
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/943oCxcRWu4
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02-14-2018 02:43 AM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
Abstract It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all detectable species. The analysis was carried out using experimental data obtained during aggregation of the 10.4 kDa Crh protein, which has been shown to involve a partially unfolded intermediate...
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01-27-2011 04:31 AM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
J Biomol NMR. 2011 Jan 21;
Authors: Etzkorn M, Böckmann A, Baldus M
It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all...
Effects of Macromolecular Cosolutes on the Kinetics of Huntingtin Aggregation Monitored by NMR Spectroscopy
Linear Mode
