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Pauli Exclusion by n→π* Interactions: Implications for Paleobiology

Jinyi Yang, Volga Kojasoy, Gerard J. Porter, Ronald T. Raines

2024ACS Central Science12 citationsDOIOpen Access PDF

Abstract

Proteins have evolved to function in an aqueous environment. Collagen, which provides the bodily scaffold for animals, has a special need to retain its integrity. This need was addressed early on, as intact collagen has been detected in dinosaur fossils, even though peptide bonds have a half-life of only ∼500 years in a neutral aqueous solution. We sought to discover the physicochemical basis for this remarkable resistance to hydrolysis. Using experimental and computational methods, we found that a main-chain acyl group can be protected from hydrolysis by an O···C=O n→π* interaction with a neighboring acyl group. These interactions engage virtually every peptide bond in a collagen triple helix. This protection, which arises from the Pauli exclusion principle, could underlie the preservation of ancient collagen.

Topics & Concepts

Pauli exclusion principlePeptideHydrolysisAqueous solutionChemistryFunction (biology)BiophysicsCombinatorial chemistryBiochemistryComputational biologyBiologyEvolutionary biologyPhysicsOrganic chemistryCondensed matter physicsCollagen: Extraction and CharacterizationBone and Dental Protein Studies
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