ArticleJournal of molecular liquids2022
Ion influence on surface water dynamics and proton exchange at protein surfaces - A unified model for transverse and longitudinal NMR relaxation dispersion.
Article in Journal of molecular liquids, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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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3 citing papers in PubMed, 6 citations in OpenAlex.
- From Power-Law to Correlation-Time Distributions: A Unified Framework for the Analysis of Nuclear Magnetic Relaxation Dispersion (NMRD) Profiles of Complex Biological Systems.Magnetic resonance in chemistry : MRC · 2026Article
- Understanding water properties in tumorous murine cells using field-cycling NMR relaxometry.Scientific reports · 2025Article
- Preparation of Polymyxin B-Functionalized Cryogels for Efficient Endotoxin Removal from Protein Solutions.Gels (Basel, Switzerland) · 2025Article
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
In all biologically relevant media, proteins interact in the presence of surrounding ions, and such interactions are water-mediated. Water molecules play a crucial role in the restructuring of proteins in solution and indeed in their biological activity. Surface water dynamics and proton exchange at protein surfaces is investigated here using NMR relaxometry, for two well-known globular proteins, lysozyme and bovine serum albumin, with particular attention to the role of surface ions. We present a unified model of surface water dynamics and proton exchange, accounting simultaneously for the observed longitudinal and transverse relaxation rates. The most notable effect of salt (0.1 M) concerns the slow surface water dynamics, related to rare water molecules embedded in energy wells on the protein surface. This response is protein-specific. On the other hand, the proton exchange time between labile protein-protons and water-protons at the protein surface seems to be very similar for the two proteins and is insensitive to the addition of salts at the concentration studied.
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