Related ArticlesSolid-state NMR sequential assignment of the ?-endorphin peptide in its amyloid form.
Biomol NMR Assign. 2016 Oct;10(2):259-68
Authors: Seuring C, Gath J, Verasdonck J, Cadalbert R, Rivier J, Böckmann A, Meier BH, Riek R
Abstract
Insights into the three-dimensional structure of hormone fibrils are crucial for a detailed understanding of how an amyloid structure allows the storage of hormones in secretory vesicles prior to hormone secretion into the blood stream. As an example for various hormone amyloids, we have studied the endogenous opioid neuropeptide ?-endorphin in one of its fibril forms. We have achieved the sequential assignment of the chemical shifts of the backbone and side-chain heavy atoms of the fibril. The secondary chemical shift analysis revealed that the ?-endorphin peptide adopts three ?-strands in its fibril state. This finding fosters the amyloid nature of a hormone at the atomic level.
[NMR paper] Solid-state NMR sequential assignment of an Amyloid-?(1-42) fibril polymorph.
Solid-state NMR sequential assignment of an Amyloid-?(1-42) fibril polymorph.
Related Articles Solid-state NMR sequential assignment of an Amyloid-?(1-42) fibril polymorph.
Biomol NMR Assign. 2016 May 10;
Authors: Ravotti F, Wälti MA, Güntert P, Riek R, Böckmann A, Meier BH
Abstract
The formation of fibrils of the amyloid-? (A?) peptide is considered to be a key event in the pathology of Alzheimer's disease (AD). The determination of a high-resolution structure of these fibrils is relevant for the understanding of the molecular...
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05-12-2016 09:30 PM
[NMR paper] Nano-mole scale sequential signal assignment by (1)H-detected protein solid-state NMR.
Nano-mole scale sequential signal assignment by (1)H-detected protein solid-state NMR.
Related Articles Nano-mole scale sequential signal assignment by (1)H-detected protein solid-state NMR.
Chem Commun (Camb). 2015 Aug 28;
Authors: Wang S, Parthasarathy S, Xiao Y, Nishiyama Y, Long F, Matsuda I, Endo Y, Nemoto T, Yamauchi K, Asakura T, Takeda M, Terauchi T, Kainosho M, Ishii Y
Abstract
We present a 3D (1)H-detected solid-state NMR (SSNMR) approach for main-chain signal assignments of 10-100 nmol of fully protonated proteins...
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09-01-2015 10:48 AM
[NMR paper] Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples.
Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples.
Related Articles Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples.
J Biomol NMR. 2015 Mar 7;
Authors: Gopinath T, Mote KR, Veglia G
Abstract
We present a new method called DAISY (Dual Acquisition orIented ssNMR spectroScopY) for the simultaneous acquisition of 2D and 3D oriented solid-state NMR experiments for membrane...
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03-10-2015 07:22 PM
Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples
Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples
Abstract
We present a new method called DAISY (Dual Acquisition orIented ssNMR spectroScopY) for the simultaneous acquisition of 2D and 3D oriented solid-state NMR experiments for membrane proteins reconstituted in mechanically or magnetically aligned lipid bilayers. DAISY utilizes dual acquisition of sine and cosine dipolar or chemical shift coherences and long living 15N longitudinal polarization to obtain two...
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03-08-2015 01:07 AM
[NMR paper] Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-? peptide: perspectives for DNP.
Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-? peptide: perspectives for DNP.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-? peptide: perspectives for DNP.
J Biomol NMR. 2013 Aug;56(4):359-63
Authors: Lopez del Amo JM, Schneider D, Loquet A, Lange A, Reif B
Abstract
Dynamic Nuclear Polarization solid-state NMR...
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05-23-2014 03:21 PM
[NMR paper] Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p.
Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p.
Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p.
Biomol NMR Assign. 2013 Aug 14;
Authors: Schütz AK, Habenstein B, Luckgei N, Bousset L, Sourigues Y, Nielsen AB, Melki R, Böckmann A, Meier BH
Abstract
Sup35p is a yeast prion and is responsible for the trait in Saccharomyces cerevisiae. With 685 amino acids, full-length soluble and fibrillar Sup35p are challenging targets for structural biology as they cannot be investigated...
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08-15-2013 07:45 PM
[NMR paper] Solid-state NMR sequential assignments of the amyloid core of Sup35pNM.
Solid-state NMR sequential assignments of the amyloid core of Sup35pNM.
Solid-state NMR sequential assignments of the amyloid core of Sup35pNM.
Biomol NMR Assign. 2013 Aug 10;
Authors: Luckgei N, Schütz AK, Habenstein B, Bousset L, Sourigues Y, Melki R, Meier BH, Böckmann A
Abstract
Sup35pNM represents the N-terminal and middle (M) domains of the yeast Saccharomyces cerevisiae prion Sup35p. This fragment is commonly used for structural and functional studies of Sup35p. We here present a solid-state NMR study of fibrils formed by this...
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08-13-2013 04:26 PM
Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP
From The DNP-NMR Blog:
Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP
Lopez del Amo, J.-M., et al., Cryogenic solid state NMR studies of fibrils of the Alzheimer’s disease amyloid-? peptide: perspectives for DNP. J. Biomol. NMR, 2013: p. 1-5.
http://www.ncbi.nlm.nih.gov/pubmed/23793606
Solid-state NMR sequential assignment of the ?-endorphin peptide in its amyloid form.
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