ReviewBiophysical chemistry2010
What can solid state NMR contribute to our understanding of protein folding?
Review in Biophysical chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed.
- Spotlight on the Nucleotide: Solid-State NMR for the Investigation of ATP Hydrolysis in the ATPase SmsC.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Structural Basis of the Membrane Association by the Conserved RocS Membrane-Targeting Sequence in Streptococcus.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Resolution in cryogenic solid state NMR: Challenges and solutions.Protein science : a publication of the Protein Society · 2024Review
- Characterization of conformational heterogeneity via higher-dimensionality, proton-detected solid-state NMR.Journal of biomolecular NMR · 2022Article
- Cryogenic Sample Loading into a Magic Angle Spinning Nuclear Magnetic Resonance Spectrometer that Preserves Cellular Viability.Journal of visualized experiments : JoVE · 2020Article
- Atomic-level insight into mRNA processing bodies by combining solid and solution-state NMR spectroscopy.Nature communications · 2019Article
- Structural analysis of the Aβ(11-42) amyloid fibril based on hydrophobicity distribution.Journal of computer-aided molecular design · 2019Article
- Photolytic labeling to probe molecular interactions in lyophilized powders.Molecular pharmaceutics · 2013Article
- Monitoring cartilage tissue engineering using magnetic resonance spectroscopy, imaging, and elastography.Tissue engineering. Part B, Reviews · 2013Review
- Structural intermediates during α-synuclein fibrillogenesis on phospholipid vesicles.Journal of the American Chemical Society · 2012Article
- Conformational disorder of membrane peptides investigated from solid-state NMR line widths and line shapes.The journal of physical chemistry. B · 2011Article
- A proton spin diffusion based solid-state NMR approach for structural studies on aligned samples.The journal of physical chemistry. B · 2011Article
- Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.Journal of biomolecular NMR · 2011Article
- Temperature jump and fast photochemical oxidation probe submillisecond protein folding.Journal of the American Chemical Society · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Complete understanding of the folding process that connects a structurally disordered state of a protein to an ordered, biochemically functional state requires detailed characterization of intermediate structural states with high resolution and site specificity. While the intrinsically inhomogeneous and dynamic nature of unfolded and partially folded states limits the efficacy of traditional X-ray diffraction and solution NMR in structural studies, solid state NMR methods applied to frozen solutions can circumvent the complications due to molecular motions and conformational exchange encountered in unfolded and partially folded states. Moreover, solid state NMR methods can provide both qualitative and quantitative structural information at the site-specific level, even in the presence of structural inhomogeneity. This article reviews relevant solid state NMR methods and their initial applications to protein folding studies. Using either chemical denaturation to prepare unfolded states at equilibrium or a rapid freezing apparatus to trap non-equilibrium, transient structural states on a sub-millisecond time scale, recent results demonstrate that solid state NMR can contribute essential information about folding processes that is not available from more familiar biophysical methods.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.