Matt Sternke

Jan 14, 2025 | biorxiv.org | Matt Sternke |Katherine W. Tripp |Doug Barrick |Johns Hopkins

AbstractThe biases revealed in protein sequence alignments have been shown to provide information related to protein structure, stability, and function. For example, sequence biases at individual positions can be used to design consensus proteins that are often more stable than naturally occurring counterparts. Likewise, correlations between pairs of residue can be used to predict protein structures.