Chapter 16 - Interactions among the three protein states
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| Year of publication | 2024 |
| Type | Chapter of a book |
| MU Faculty or unit | |
| Citation | |
| Description | Interactions between the three states of proteins (structured, intrinsically disordered, and phase separated) can be probed by a variety of experimental methods. First, we review fundamental physical forces determining structural features and intermolecular interactions of all three states of proteins. We classify individual contributions of the interactions, comment on their theoretical treatment, stress the importance of water as a solvent, and discuss the hierarchy of protein structures. Then we briefly mention methods of structure determination at the atomic resolution and describe in more detail selected methods probing specific features of intra- and intermolecular protein interactions. The selection includes various methods of nuclear magnetic resonance spectroscopy (including analysis of chemical shifts, relaxation effects, and measurements of translational diffusion and proton exchange) and methods reflecting hydrodynamic behavior, namely, analytical ultracentrifugation and small-angle X-ray scattering. The text does not have an ambition to provide actual protocols or a complete list of applications but tries to comment on the use of the methods for the three states of proteins. |
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