Evidence map›Paper›PMID 42442050›Full record

ArticleBiophysical chemistry2026

Enhanced solid-state NMR sensitivity of α-synuclein fibrils using a MAS cryoprobe.

Malitha C Dickwella Widanage, Barbara Perrone, Jhinuk Saha, Riqiang Fu, Jochem Struppe, Ryan P McGlinchey, Robert W Schurko, Ayyalusamy Ramamoorthy

Abstract read
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In one paragraph

Article in Biophysical chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Malitha C Dickwella WidanageNational High Magnetic Field Laboratory, 1800 E. Paul Dirac Drive, Tallahassee, FL 32310, United States of America; Department of Chemical and Biomedical Engineering, FAMU-FSU College of Engineering, Tallahassee, FL 32310, United States of America; Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32304, United States of America.
Barbara PerroneBruker Biospin, Fällanden, Switzerland.
Jhinuk SahaNational High Magnetic Field Laboratory, 1800 E. Paul Dirac Drive, Tallahassee, FL 32310, United States of America; Department of Chemical and Biomedical Engineering, FAMU-FSU College of Engineering, Tallahassee, FL 32310, United States of America; Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32304, United States of America.
Riqiang FuNational High Magnetic Field Laboratory, 1800 E. Paul Dirac Drive, Tallahassee, FL 32310, United States of America.
Jochem StruppeBruker, Billerica, United States of America.
Ryan P McGlincheyLaboratory of Protein Conformation and Dynamics, Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, United States.
Robert W SchurkoNational High Magnetic Field Laboratory, 1800 E. Paul Dirac Drive, Tallahassee, FL 32310, United States of America; Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32306, United States.
Ayyalusamy RamamoorthyNational High Magnetic Field Laboratory, 1800 E. Paul Dirac Drive, Tallahassee, FL 32310, United States of America; Department of Chemical and Biomedical Engineering, FAMU-FSU College of Engineering, Tallahassee, FL 32310, United States of America; Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32304, United States of America; Biophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, United States. Electronic address: aramamoorthy@fsu.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Solid-state NMR spectroscopy is increasingly used to investigate the structure and dynamics of a wide range of chemical, material, and biological systems. Although limited sensitivity has long posed a major challenge, the recently developed MAS cryoprobe substantially alleviates this limitation. By enhancing the signal-to-noise (S/N) ratio without requiring sample freezing, the MAS cryoprobe is particularly well suited for studies of non-isotropic systems, including rigid solids (e.g., amyloid fibrils), semi-solids (e.g., membrane mimetics), and soft materials (e.g., nanodiscs and hydrogels). In this study, we demonstrate the enhanced sensitivity of solid-state NMR experiments on α-synuclein fibrils using a MAS cryoprobe. Compared with a conventional MAS probe, substantial improvements in S/N were observed in CPMAS, refocused INEPT, and 2D

Indexed as

alpha-SynucleinAmyloidNuclear Magnetic Resonance, BiomolecularHumansSignal-To-Noise Ratioalpha-SynucleinAmyloid

Identifiers

PMID42442050

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.