A Method for Assessing the Robustness of Protein Structures by Randomizing Packing Interactions
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DOI: 10.3389/fmolb.2022.849272
Abstract: Many single-domain proteins are not only stable and water-soluble, but they also populate few to no intermediates during folding. This reduces interactions between partially folded proteins, misfolding, and aggregation, and makes the proteins tractable in… read more here.
Keywords: protein structures; structures randomizing; robustness protein; method assessing ... See more keywords