Title | Hydrogen Mobility and Protein-Water Interactions in Proteins in the Solid State. |
Publication Type | Journal Article |
Year of Publication | 2017 |
Authors | Tompa, K., M. Bokor, D. Ágner, D. Iván, D. Kovacs, T. Verebélyi, and P. Tompa |
Journal | Chemphyschem |
Volume | 18 |
Issue | 6 |
Pagination | 677-682 |
Date Published | 2017 Mar 17 |
ISSN | 1439-7641 |
Keywords | Arabidopsis Proteins, Hydrogen, Muramidase, Water |
Abstract | In this work the groundwork is laid for characterizing the mobility of hydrogen-hydrogen pairs (proton-proton radial vectors) in proteins in the solid state that contain only residual water. In this novel approach, we introduce new ways of analyzing and interpreting data: 1) by representing hydrogen mobility (HM) and melting diagram (MD) data recorded by wide-line H NMR spectroscopic analysis as a function of fundamental temperature (thermal excitation energy); 2) by suggesting a novel mode of interpretation of these parameters that sheds light on details of protein-water interactions, such as the exact amount of water molecules and the distribution of barrier potentials pertaining to their rotational and surface translational mobility; 3) by relying on directly determined physical observables. We illustrate the power of this approach by studying the behavior of two proteins, the structured enzyme lysozyme and the intrinsically disordered ERD14. |
DOI | 10.1002/cphc.201601136 |
Alternate Journal | Chemphyschem |
PubMed ID | 28066974 |
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