Rheostatic contributions to protein stability can obscure a position's functional role
Pierce T. O'Neil,
Liskin Swint‐Kruse,
Aron W. Fenton
Abstract:Rheostat positions, which can be substituted with various amino acids to tune protein function across a range of outcomes, are a developing area for advancing personalized medicine and bioengineering. Current methods cannot accurately predict which proteins contain rheostat positions or their substitution outcomes. To compare the prevalence of rheostat positions in homologs, we previously investigated their occurrence in two pyruvate kinase (PYK) isozymes. Human liver PYK contained numerous rheostat positions … Show more
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