ArticleBiochemistry2013
What's in your buffer? Solute altered millisecond motions detected by solution NMR.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 11 papers.
What it found
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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.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Parameter Reliability and Understanding Enzyme Function.Molecules (Basel, Switzerland) · 2022Review
- Discovery of a hidden transient state in all bromodomain families.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Allomorphy as a mechanism of post-translational control of enzyme activity.Nature communications · 2020Article
- Addressing a Common Misconception: Ammonium Acetate as Neutral pH "Buffer" for Native Electrospray Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017Article
- Characterisation of three fungal glucuronoyl esterases on glucuronic acid ester model compounds.Applied microbiology and biotechnology · 2017Article
- Entire-Dataset Analysis of NMR Fast-Exchange Titration Spectra: A MgThe journal of physical chemistry. B · 2016Article
- Optimization of protein samples for NMR using thermal shift assays.Journal of biomolecular NMR · 2016Article
- Cofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway.Journal of the American Chemical Society · 2015Article
- Assignments of RNase A by ADAPT-NMR and enhancer.Biomolecular NMR assignments · 2015Article
- Complexity of protein energy landscapes studied by solution NMR relaxation dispersion experiments.The journal of physical chemistry. B · 2015Article
- Protein-Inhibitor Interaction Studies Using NMR.Applications of NMR spectroscopyArticle
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
To date, little work has been conducted on the relationship between solute and buffer molecules and conformational exchange motion in enzymes. This study uses solution NMR to examine the effects of phosphate, sulfate, and acetate in comparison to MES- and HEPES-buffered references on the chemical shift perturbation and millisecond, chemical, or conformational exchange motions in the enzyme ribonuclease A (RNase A), triosephosphate isomerase (TIM) and HisF. The results indicate that addition of these solutes has a small effect on (1)H and (15)N chemical shifts for RNase A and TIM but a significant effect for HisF. For RNase A and TIM, Carr-Purcell-Meiboom-Gill relaxation dispersion experiments, however, show significant solute-dependent changes in conformational exchange motions. Some residues show loss of millisecond motions relative to the reference sample upon addition of solute, whereas others experience an enhancement. Comparison of exchange parameters obtained from fits of dispersion data indicates changes in either or both equilibrium populations and chemical shifts between conformations. Furthermore, the exchange kinetics are altered in many cases. The results demonstrate that common solute molecules can alter observed enzyme millisecond motions and play a more active role than what is routinely believed.
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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.