Abstract
Native structures of many proteins have been solved experimentally or predicted with increasing accuracy using evolutionary couplings and machine learning. However, no current approach is well-suited for elucidating misfolded, partially disordered, or transient conformational states. Such altered conformations are of high interest because they drive protein misfolding diseases, determine success in protein design efforts, and provide evolutionary routes toward conformational switching. To discover non-native structures a protein may adopt (upon random fluctuation, environmental perturbation, or mutation) and to map them to their molecular, cellular, or organismal phenotypic consequences, we have developed a new experimental structural technique: high-throughput disulfide scanning (HTDS).
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