|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|
|Date Published||2017 Mar 17|
|Keywords||Arabidopsis Proteins, Hydrogen, Muramidase, Water|
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.
Hydrogen Mobility and Protein-Water Interactions in Proteins in the Solid State.