ReviewMethods in enzymology2019
NMR Methods for Characterizing the Basic Side Chains of Proteins: Electrostatic Interactions, Hydrogen Bonds, and Conformational Dynamics.
Review in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 26 citations in OpenAlex.
- At the core of the interaction: Probing charged side chains in flexible protein regions with simultaneous nuclear magnetic resonance experiments.Protein science : a publication of the Protein Society · 2026Article
- CH•••S hydrogen bonds drive molecular recognition of ergothioneine by the microbial transporter.Science advances · 2026Article
- AlphaFold 3 accurately models natural variants ofMicrobiology spectrum · 2025Article
- Synthesis of SelectivelyChemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Solid state NMR spectral editing of histidine, arginine and lysine using Hadamard encoding.Journal of biomolecular NMR · 2025Article
- Physical and Structural Properties of Chitosan-Squid Gelatin Hydrogels.Gels (Basel, Switzerland) · 2025Article
- UCBShift 2.0: Bridging the Gap from Backbone to Side Chain Protein Chemical Shift Prediction for Protein Structures.Journal of the American Chemical Society · 2024Article
- NMR detection and conformational dependence of two, three, and four-bond isotope shifts due to deuteration of backbone amides.Journal of biomolecular NMR · 2023Article
- Slow Rotational Dynamics of Cytosine NHBiochemistry · 2022Article
- Hindered Rotations of Protein Asparagine/Glutamine Side-Chain NHThe journal of physical chemistry letters · 2021Article
- Minimizing Pervasive Artifacts in 4D Covariance Maps for Protein Side Chain NMR Assignments.The journal of physical chemistry. A · 2021Article
- Quantifying and visualizing weak interactions between anions and proteins.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Experimental approaches for investigating ion atmospheres around nucleic acids and proteins.Computational and structural biotechnology journal · 2021Review
- Racemic phosphorothioate as a tool for NMR investigations of protein-DNA complexes.Journal of biomolecular NMR · 2020Article
- Hydrogen-exchange kinetics studied through analysis of self-decoupling of nuclear magnetic resonance.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020Article
- NMR Observation of Intermolecular Hydrogen Bonds between Protein Tyrosine Side-Chain OH and DNA Phosphate Groups.The journal of physical chemistry. B · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
NMR spectroscopy is a powerful tool for studying protein dynamics. Conventionally, NMR studies on protein dynamics have probed motions of protein backbone NH, side-chain aromatic, and CH
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.