Self-assembly of amyloid-? peptides leads to oligomers, protofibrils, and fibrils that are likely instigators of neurodegeneration in Alzheimer's disease. We report results of time-resolved solid state nuclear magnetic resonance (ssNMR) and light scattering experiments on 40-residue amyloid-? (A?40) that provide structural information for oligomers that form on time scales from 0.7 ms to 1.0 h after initiation of self-assembly by a rapid pH drop. Low-temperature ssNMR spectra of freeze-trapped...
[NMR paper] Surface Accessibility of an Intrinsically Disordered Protein Probed by 2D Time-Resolved Laser-Assisted NMR Spectroscopy
Surface Accessibility of an Intrinsically Disordered Protein Probed by 2D Time-Resolved Laser-Assisted NMR Spectroscopy
Probing the protein surface accessibility of different residues is a powerful way of characterizing the overall conformation of intrinsically disordered proteins (IDPs). We present a two-dimensional (2D) time-resolved photo-CIDNP (TR-CIDNP) experiment suitable for IDP analysis. Pulse stretching of high-power laser pulses, band-selective decoupling of ^(13)C^(?), and simultaneous application of radiofrequency and laser pulses were implemented to quantitatively analyze the...
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09-11-2022 10:03 PM
[NMR paper] Time-resolved solid state NMR of biomolecular processes with millisecond time resolution
Time-resolved solid state NMR of biomolecular processes with millisecond time resolution
We review recent efforts to develop and apply an experimental approach to the structural characterization of transient intermediate states in biomolecular processes that involve large changes in molecular conformation or assembly state. This approach depends on solid state nuclear magnetic resonance (ssNMR) measurements that are performed at very low temperatures, typically 25-30 K, with signal enhancements from dynamic nuclear polarization (DNP). This approach also involves novel technology for...
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[NMR paper] Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase.
Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase.
Related Articles Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase.
J Am Chem Soc. 2020 Dec 07;:
Authors: Jeon J, Yau WM, Tycko R
Abstract
Calmodulin (CaM) mediates a wide range of biological responses to changes in...
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12-08-2020 01:36 PM
[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] Light-induced uncaging for time-resolved observations of biochemical reactions by MAS NMR spectroscopy.
Light-induced uncaging for time-resolved observations of biochemical reactions by MAS NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7388-69-wiley-full-text.png Related Articles Light-induced uncaging for time-resolved observations of biochemical reactions by MAS NMR spectroscopy.
Chemistry. 2020 Apr 02;:
Authors: de Mos J, Jakob A, Becker-Baldus J, Heckel A, Glaubitz C
Abstract
Light-induced activation of biomolecules by uncaging of photolabile protection groups...
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04-03-2020 09:41 PM
[NMR paper] Hydrogen bond strength in membrane proteins probed by time-resolved (1)H-detected solid-state NMR and MD simulations.
Hydrogen bond strength in membrane proteins probed by time-resolved (1)H-detected solid-state NMR and MD simulations.
Related Articles Hydrogen bond strength in membrane proteins probed by time-resolved (1)H-detected solid-state NMR and MD simulations.
Solid State Nucl Magn Reson. 2017 Mar 18;:
Authors: Medeiros-Silva J, Jekhmane S, Baldus M, Weingarth M
Abstract
(1)H-detected solid-state NMR in combination with (1)H/(2)D exchange steps allows for the direct identification of very strong hydrogen bonds in membrane proteins....