Beyond the Native State: From Protein Structure to Function Through Energy Landscapes and Conformational Ensembles

Authors

  • Ishaan Goswami University of Ottawa, Ottawa, ON, Canada
  • Isra F. Omar University of Ottawa, Ottawa, ON, Canada

DOI:

https://doi.org/10.18192/osurj.v5i1.8045

Abstract

Rather than viewing protein folding as the formation of a single native structure, modern biophysics describes proteins as statistical ensembles of interconverting conformations whose populations are determined by thermodynamics, kinetics, and the energy landscape imposed by molecular interactions. Within this framework, folding is not considered a discrete event, but a dynamic process. When placed in a cellular context, these dynamic conformational ensembles are coupled to protein function and are directly influenced by the intracellular environment and interacting proteins. Protein folding and function still follow biophysical laws, albeit with varying significances, and can be described using kinetic models of intra- and intermolecular interactions. This review explores the biophysical, biochemical, and cellular determinants of protein folding, specifically highlighting that protein behaviour is a property of ensemble dynamics and the intracellular environment.

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Published

2026-06-17

Issue

Vol. 5 No. 1 (2026)

Section

Reviews

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