The tropomyosin 1 isoform I/C C-terminal domain (Tm1-LC) fibril structure is studied jointly with cryogenic electron microscopy (cryo-EM) and solid state nuclear magnetic resonance (NMR). This study demonstrates the complementary nature of these two structural biology techniques. Chemical shift assignments from solid state NMR are used to determine the secondary structure at the level of individual amino acids, which is faithfully seen in cryo-EM reconstructions. Additionally, solid state NMR demonstrates that the region not observed in the reconstructed cryo-EM density is primarily in a highly mobile random coil conformation rather than adopting multiple rigid conformations. Overall, this study illustrates the benefit of investigations combining cryo-EM and solid state NMR to investigate protein fibril structure.
[NMR paper] Cryo-EM and Solid State NMR Together Provide a More Comprehensive Structural Investigation of Protein Fibrils
Cryo-EM and Solid State NMR Together Provide a More Comprehensive Structural Investigation of Protein Fibrils
The Tropomyosin 1 isoform I/C C-terminal domain (Tm1-LC) fibril structure is studied jointly with cryogenic electron microscopy (cryo-EM) and solid state nuclear magnetic resonance (NMR). This study demonstrates the complementary nature of these two structural biology techniques. Chemical shift assignments from solid state NMR are used to determine the secondary structure at the level of individual amino acids, which is faithfully seen in cryo-EM reconstructions. Additionally,...
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06-10-2024 10:40 AM
[NMR paper] Structural and dynamical investigation of histone H2B in well-hydrated nucleosome core particles by solid-state NMR
Structural and dynamical investigation of histone H2B in well-hydrated nucleosome core particles by solid-state NMR
H2A-H2B dimer is a key component of nucleosomes and an important player in chromatin biology. Here, we characterized the structure and dynamics of H2B in precipitated nucleosome core particles (NCPs) with a physiologically relevant concentration using solid-state NMR. Our recent investigation of H3-H4 tetramer determined its unique dynamic properties and the present work provides a deeper understanding of the previously observed dynamic networks in NCP that is potentially...
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06-28-2023 01:01 AM
[NMR paper] Emerging Structural Understanding of Amyloid Fibrils by Solid-State NMR.
Emerging Structural Understanding of Amyloid Fibrils by Solid-State NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Emerging Structural Understanding of Amyloid Fibrils by Solid-State NMR.
Trends Biochem Sci. 2017 Oct;42(10):777-787
Authors: Meier BH, Riek R, Böckmann A
Abstract
Amyloid structures at atomic resolution have remained elusive mainly because of their extensive polymorphism and because their polymeric properties have hampered...
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10-12-2017 02:58 PM
[NMR paper] Structural Polymorphism of Alzheimer's ?-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.
Structural Polymorphism of Alzheimer's ?-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.
Structural Polymorphism of Alzheimer's ?-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.
J Am Chem Soc. 2016 Jul 14;
Authors: Elkins MR, Wang T, Nick M, Jo H, Lemmin T, Prusiner SB, DeGrado WF, Stoehr J, Hong M
Abstract
The amyloid-? (A?) peptide of the Alzheimer's disease (AD) forms polymorphic fibrils on the micrometer scale and molecular scale. Various fibril growth conditions have been...
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07-16-2016 04:54 AM
Structural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy.
Structural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy.
Structural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy.
J Mol Biol. 2011 Jul 13;
Authors: Schneider R, Schumacher MC, Mueller H, Nand D, Klaukien V, Heise H, Riedel D, Wolf G, Behrmann E, Raunser S, Seidel R, Engelhard M, Baldus M
Protein aggregation via polyglutamine stretches occurs in a number of severe neurodegenerative diseases such as Huntington's disease. We have investigated fibrillar aggregates of polyglutamine peptides...
Solid-state NMR and SAXS studies provide a structural basis for the activation of alp
Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers.
Related Articles Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers.
Nat Struct Mol Biol. 2010 Aug 29;
Authors: Jehle S, Rajagopal P, Bardiaux B, Markovic S, Kühne R, Stout JR, Higman VA, Klevit RE, van Rossum BJ, Oschkinat H
The small heat shock protein alphaB-crystallin (alphaB) contributes to cellular protection against stress. For decades, high-resolution structural studies on...
Cryo-EM and solid state NMR together provide a more comprehensive structural investigation of protein fibrils
Linear Mode
