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Localisation of thermal energy, topological disorder and the art of regulation in biochemistry
This seminar proposes to address an atomic mechanism describing how part of the regulation of biochemistry emerges in proteins and protein assemblies. A physical description linking the topology of macromolecular complexes to their biochemical function will be exposed through dynamic effects arising from fold-encoded localized phonons. We thus show that irregular macromolecules intrinsically possess information or entropy transport networks involving distinct molecular domains. These evolutionarily driven distal feedbacks between atomic fluctuations explain the basis of three of the most fundamental functions of proteins, namely catalysis, transmembrane communication, and the inhibitory effects of drug molecules. This theoretical approach provides a microscopic understanding of how nature exploits structural disorder to produce molecules with fold-encoded biochemical complexity, thus providing a new tool for controlling protein and nucleoprotein complexes in general.