Transition-State Compressibility and Activation Volume of Transient Protein Conformational Fluctuations

Matthias Dreydoppel, Brita Dorn, Kristofer Modig, Mikael Akke, Ulrich Weininger

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskriftPeer review


Proteins are dynamic entities that intermittently depart from their ground-state structures and undergo conformational transitions as a critical part of their functions. Central to understanding such transitions are the structural rearrangements along the connecting pathway, where the transition state plays a special role. Using NMR relaxation at variable temperature and pressure to measure aromatic ring flips inside a protein core, we obtain information on the structure and thermodynamics of the transition state. We show that the isothermal compressibility coefficient of the transition state is similar to that of short-chain hydrocarbon liquids, implying extensive local unfolding of the protein. Our results further indicate that the required local volume expansions of the protein can occur not only with a net positive activation volume of the protein, as expected from previous studies, but also with zero activation volume by compaction of remote void volume, when averaged over the ensemble of states.
Sidor (från-till)833-842
Antal sidor10
TidskriftJACS Au
StatusPublished - 2021 juni 3

Ämnesklassifikation (UKÄ)

  • Fysikalisk kemi
  • Strukturbiologi


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