1. Thermostability of Salt Bridges versus Hydrophobic Interactions in Proteins Probed by Statistical Potentials
fork-fork / fork-stick salt bridge
These two minima correspond to two geometries: the fork-fork geometry, where the side chains point toward each other, and the fork-stick geometry, which involves the N(epsilon) side chain atom of Arg. These two types of salt bridges were determined to be significantly more stabilizing at high temperature.
2. Configurational entropy elucidates the role of salt-bridge networks in protein thermostability
Detailed knowledge of how networks of surface salt bridges contribute to protein thermal stability is essential not only to understand protein structure and function but also to design thermostable proteins for industrial applications.
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