Title : Multiscale Water Dynamics on Protein Surfaces: Protein-Specific Response to Surface Ions.

Pub. Date : 2021 Aug 12

PMID : 34342225






3 Functional Relationships(s)
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1 In the present study, we combine field-dependent NMR relaxation (NMRD) and theory to probe water dynamics on the surface of proteins in concentrated aqueous solutions of hen egg-white lysozyme (LZM) and bovine serum albumin (BSA). Water lysozyme Homo sapiens
2 In the present study, we combine field-dependent NMR relaxation (NMRD) and theory to probe water dynamics on the surface of proteins in concentrated aqueous solutions of hen egg-white lysozyme (LZM) and bovine serum albumin (BSA). Water lysozyme Homo sapiens
3 The experiments reveal that the presence of salts (NaCl or NaI) leads to an opposite ion-specific response for the two proteins: an addition of salt to LZM solutions increases water relaxation rates with respect to the salt-free case, while for BSA solutions, a decrease is observed. Water lysozyme Homo sapiens