Functional tunability from a distance: Rheostat positions influence allosteric coupling between two distant binding sites

Abstract excerpt

For protein mutagenesis, a common expectation is that important positions will behave like on/off “toggle” switches ( i.e. , a few substitutions act like wildtype, most abolish function). However, there exists another class of important positions that manifests a wide range of functional outcomes upon substitution: “rheostat” positions. Previously, we evaluated rheostat positions located near the allosteric bindi...

Topics

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• Alanine
• Algorithms
• Allosteric Regulation
• Computational Biology
• Crystallography, X-Ray
• Enzyme Activation
• Models, Molecular
• Pyruvate Kinase

Identifiers and source

Literature Corpus work

a51c1b52-e77d-5294-87e0-2b94b10e5f8b

DOI

10.1101/632422