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Proteins? Evolution upon Point Mutations
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DOI：10.1021/acsomega.2c01407.png)
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Abstract
En 中文
As the reader must be already aware, state-of-the-art protein folding prediction methods have reached a smashing success in their goal of accurately determining the threedimensional structures of proteins. Yet, a solution to simple problems such as the effects of protein point mutations on their (i) energy nativelike conformations; and (iv) metamorphism propensity and, hence, their evolvability, remains as an unsolved problem. As a plausible solution to the latter, some properties of the amide hydrogen-deuterium exchange, a highly sensitive probe of the structure, stability, and folding of proteins, are assessed from a new perspective. The preliminary results indicate that the protein marginal stability change upon point mutations provides the necessary and sufficient information to estimate, through a Boltzmann factor, the evolution of the amide hydrogen exchange protection factors and, consequently, that of the ensemble of folded conformations coexisting with the native state. This work contributes to our general understanding of the effects of point mutations on proteins and may spur significant progress in our efforts to develop methods to determine the appearance of new folds and functions accurately.
Keywords:
STATE HYDROGEN-EXCHANGE
METAMORPHIC PROTEINS
DIRECTED EVOLUTION
STABILITY
EPISTASIS
PREDICTION
ENERGY
CONFORMATIONS
FLUCTUATIONS
ROBUSTNESS
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