[NMR paper] The N-Terminal Domain of Abeta(40)-Amyloid Fibril: The MOMD Perspective of its Dynamic Structure from NMR Lineshape Analysis
The N-Terminal Domain of Abeta(40)-Amyloid Fibril: The MOMD Perspective of its Dynamic Structure from NMR Lineshape Analysis
We have developed the stochastic microscopic-order-macroscopic-disorder (MOMD) approach for elucidating dynamic structures in the solid-state from ²H NMR lineshapes. In MOMD, the probe experiences an effective/collective motional mode. The latter is described by a potential, u, which represents the local spatial-restrictions, a local-motional diffusion tensor, R, and key features of local geometry. Previously we applied MOMD to the well-structured core domain of the...
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02-08-2022 01:38 PM
[NMR paper] Water Dynamics in Whey-Protein-Based Composite Hydrogels by Means of NMR Relaxometry
Water Dynamics in Whey-Protein-Based Composite Hydrogels by Means of NMR Relaxometry
Whey-protein-isolate-based composite hydrogels with encapsulated black carrot (Daucus carota) extract were prepared by heat-induced gelation. The hydrogels were blended with gum tragacanth, pectin and xanthan gum polysaccharides for modulating their properties. ¹H spin-lattice relaxation experiments were performed in a broad frequency range, from 4 kHz to 30 MHz, to obtain insight into the influence of the different polysaccharides and of the presence of black carrot on dynamical properties of...
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09-29-2021 12:23 PM
[NMR paper] Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR.
Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR.
Related Articles Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR.
Biophys Rev. 2018 May 31;:
Authors: Martial B, Lefèvre T, Auger M
Abstract
It is well established that amyloid proteins play a primary role in neurodegenerative diseases. Alzheimer's, Parkinson's, type II diabetes, and Creutzfeldt-Jakob's...
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06-02-2018 12:52 PM
An in vivo platform for identifying inhibitors of protein aggregation - Nature.com
An in vivo platform for identifying inhibitors of protein aggregation - Nature.com
http://www.bionmr.com//t0.gstatic.com/images?q=tbn:ANd9GcSLHh_MJ51qJn95VA8NpN9DXS6GnDXVnuOykdY7XpQhQYmpJvEInY-BuBS86dh26OpLGCL-rexl
Nature.com
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An in vivo platform for identifying inhibitors of protein aggregation
Nature.com
We show that the system can be used to detect aggregation-prone sequences and to screen for inhibitors that prevent protein aggregation, using as examples human and rat islet amyloid polypeptide (hIAPP and rIAPP, respectively), amyloid β1â??40...
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12-16-2015 08:50 AM
[NMR paper] NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain.
NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain.
Related Articles NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain.
Biomol NMR Assign. 2013 Nov 15;
Authors: Kaplan AR, Maciejewski MW, Olson R, Alexandrescu AT
Abstract
Pathogenic bacteria secrete pore-forming toxins (PFTs) to selectively defend against immune cells and to break through cellular barriers in the host. Understanding how PFTs attack cell membranes is not only essential for therapeutic intervention but for...
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11-16-2013 03:14 PM
[NMR paper] NMR structure note: repetitive domain of aciniform spidroin 1 from Nephila antipodiana.
NMR structure note: repetitive domain of aciniform spidroin 1 from Nephila antipodiana.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR structure note: repetitive domain of aciniform spidroin 1 from Nephila antipodiana.
J Biomol NMR. 2012 Dec;54(4):415-20
Authors: Wang S, Huang W, Yang D
PMID: 23129012
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05-15-2013 03:12 PM
NMR structure note: repetitive domain of aciniform spidroin 1 from Nephila antipodiana
NMR structure note: repetitive domain of aciniform spidroin 1 from Nephila antipodiana
NMR structure note: repetitive domain of aciniform spidroin 1 from Nephila antipodiana
Content Type Journal Article
Category NMR structure note
Pages 1-6
DOI 10.1007/s10858-012-9679-5
Authors
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11-10-2012 01:53 AM
NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1.
NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1.
NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1.
Biomol NMR Assign. 2010 Dec 10;
Authors: Parnham S, Gaines WA, Duggan BM, Marcotte WR, Hennig M
The building blocks of spider dragline silk are two fibrous proteins secreted from the major ampullate gland named spidroins 1 and 2 (MaSp1, MaSp2). These proteins consist of a large central domain composed of approximately 100 tandem copies of a 35-40 amino acid repeat sequence. Non-repetitive N and...