Zinc ions are commonly involved in enzyme catalysis and protein structure stabilization, but their coordination geometry of zinc-protein complex is rarely determined. Here, in this chapter, we introduce a systematic solid-state NMR approach to determine the oligomeric assembly and Zn^(2+) coordination geometry of a de novo designed amyloid fibrils that catalyze zinc dependent ester hydrolysis. NMR chemical shifts and intermolecular contacts confirm that the peptide forms parallel-in-register...
[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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[NMR paper] Solid state NMR assignments of a human ?-III immunoglobulin light chain amyloid fibril.
Solid state NMR assignments of a human ?-III immunoglobulin light chain amyloid fibril.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Solid state NMR assignments of a human ?-III immunoglobulin light chain amyloid fibril.
Biomol NMR Assign. 2020 Sep 18;:
Authors: Pradhan T, Annamalai K, Sarkar R, Hegenbart U, Schönland S, Fändrich M, Reif B
Abstract
The aggregation of antibody light chains is linked to systemic light...
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09-21-2020 05:44 PM
[NMR paper] 3D Structure Determination of Amyloid Fibrils using Solid-State NMR Spectroscopy.
3D Structure Determination of Amyloid Fibrils using Solid-State NMR Spectroscopy.
3D Structure Determination of Amyloid Fibrils using Solid-State NMR Spectroscopy.
Methods. 2018 Apr 05;:
Authors: Loquet A, El Mammeri N, Stanek J, Berbon M, Bardiaux B, Pintacuda G, Habenstein B
Abstract
The amyloid fold is structurally characterized by a typical cross-? architecture, which is under debate to represent an energy-favourable folding state that many globular or natively unfolded proteins can adopt. Being initially solely associated...
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04-09-2018 11:12 AM
Zinc-binding structure of a catalytic amyloid from solid-state NMR [Biophysics and Computational Biology]
Zinc-binding structure of a catalytic amyloid from solid-state NMR
Myungwoon Lee, Tuo Wang, Olga V. Makhlynets, Yibing Wu, Nicholas F. Polizzi, Haifan Wu, Pallavi M. Gosavi, Jan Stohr, Ivan V. Korendovych, William F. DeGrado, Mei Hong...
Date: 2017-06-13
Throughout biology, amyloids are key structures in both functional proteins and the end product of pathologic protein misfolding. Amyloids might also represent an early precursor in the evolution of life because of their small molecular size and their ability to self-purify and catalyze chemical reactions. They also provide attractive...
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06-13-2017 09:46 PM
[NMR paper] Zinc-binding structure of a catalytic amyloid from solid-state NMR.
Zinc-binding structure of a catalytic amyloid from solid-state NMR.
Related Articles Zinc-binding structure of a catalytic amyloid from solid-state NMR.
Proc Natl Acad Sci U S A. 2017 May 31;:
Authors: Lee M, Wang T, Makhlynets OV, Wu Y, Polizzi NF, Wu H, Gosavi PM, Stöhr J, Korendovych IV, DeGrado WF, Hong M
Abstract
Throughout biology, amyloids are key structures in both functional proteins and the end product of pathologic protein misfolding. Amyloids might also represent an early precursor in the evolution of life because of...
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06-02-2017 08:33 PM
[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] Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Related Articles Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Annu Rev Biophys. 2013 Mar 22;
Authors: Comellas G, Rienstra CM
Abstract
Protein structure determination methods using magic-angle spinning solidstate nuclear magnetic resonance (MAS SSNMR) have experienced a remarkable...
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03-27-2013 03:33 PM
Solid-State NMR Studies of Amyloid Fibril Structure.
Solid-State NMR Studies of Amyloid Fibril Structure.
Solid-State NMR Studies of Amyloid Fibril Structure.
Annu Rev Phys Chem. 2010 Apr 2;
Authors: Tycko R
Current interest in amyloid fibrils stems from their involvement in neurodegenerative and other diseases and from their role as an alternative structural state for many peptides and proteins. Solid-state nuclear magnetic resonance (NMR) methods have the unique capability of providing detailed structural constraints for amyloid fibrils, sufficient for the development of full molecular models. In...
Solid-state NMR spectroscopic analysis for structure determination of a zinc-bound catalytic amyloid fibril
Linear Mode
