ArticleProceedings of the National Academy of Sciences of the United States of America2010
Investigation of protein conformation and interactions with salts via X-ray absorption spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. 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 10 papers.
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10 citing papers in PubMed, 37 citations in OpenAlex.
- X-ray absorption spectroscopy of lanmodulin-derived peptides bound to rare earth elements.Journal of synchrotron radiation · 2025Article
- The influence of KCl concentration on the gelation of myofibrillar protein giant squid (Frontiers in nutrition · 2022Article
- NitrogenThe journal of physical chemistry letters · 2021Article
- The Interfacial Interactions of Glycine and Short Glycine Peptides in Model Membrane Systems.International journal of molecular sciences · 2020Article
- An insight into hydration structure of sodium glycinate from ab initio quantum chemical study.Journal of molecular modeling · 2015Article
- Quantitative characterization of non-classic polarization of cations on clay aggregate stability.PloS one · 2015Article
- Probing ion-specific effects on aqueous acetate solutions: Ion pairing versus water structure modifications.Structural dynamics (Melville, N.Y.) · 2014Article
- L-Edge X-ray Absorption Spectroscopy of Dilute Systems Relevant to Metalloproteins Using an X-ray Free-Electron Laser.The journal of physical chemistry letters · 2013Article
- Salt effects on the conformational stability of the visual G-protein-coupled receptor rhodopsin.Biophysical journal · 2011Article
- Effects of select anions from the Hofmeister series on the gas-phase conformations of protein ions measured with traveling-wave ion mobility spectrometry/mass spectrometry.Journal of the American Society for Mass Spectrometry · 2011Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nitrogen K-edge spectra of aqueous triglycine were measured using liquid microjets, and the effects of Hofmeister-active salts on the spectra were observed. Spectra simulated using density functional theory, sampled from room temperature classical molecular dynamics trajectories, capture all major features in the measured spectra. The spectrum of triglycine in water is quite similar to that in the presence of chaotropic sodium bromide (and other halides), which raises the solubility of proteins. However, a new feature is found when kosmotropic Na(2)SO(3), which lowers solubility, is present; this feature results from excitations of the nitrogen atom in the terminal amino group of triglycine. Both direct interactions between this salt and the protonated amino terminus, as well as corresponding changes in the conformational dynamics of the system, contribute to this new feature. These molecular measurements support a different mechanism for the Hofmeister effect than has previously been suggested based on thermodynamic measurements. It is also shown that near edge X-ray absorption fine structure (NEXAFS) is sensitive to strong direct interaction between certain salts and charged peptides. However, by investigating the sensitivity of NEXAFS to the extreme structural differences between model beta-sheets and alpha-helices, we conclude that this technique is relatively insensitive to secondary structure of peptides and proteins.
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