A billion years of evolution manifest in nanosecond protein dynamics
Philipp J. Heckmeier, Jeannette Ruf, Charlotte Rochereau, and Peter, Hamm

TL;DR
This study investigates how billion-year evolutionary divergence influences nanosecond protein dynamics across homologs, revealing conserved kinetic footprints and subtle temporal shifts linked to evolutionary history, with implications for molecular paleontology.
Contribution
It provides the first detailed comparison of ultrafast protein dynamics across species separated by nearly a billion years, highlighting conserved processes and evolutionary effects.
Findings
Identified three conserved dynamic activity points in protein complexes.
Discovered a subtle temporal shift correlating with evolutionary divergence.
Proposed a new approach linking protein dynamics to molecular paleontology.
Abstract
Protein dynamics form a critical bridge between protein structure and function, yet the impact of evolution on ultrafast processes inside proteins remains enigmatic. This study delves deep into nanosecond-scale protein dynamics of a structurally and functionally conserved protein across species separated by almost a billion years, investigating ten homologs in complex with their ligand. By inducing a photo-triggered destabilization of the ligand inside the binding pocket, we resolved distinct kinetic footprints for each homolog via transient infrared spectroscopy . Strikingly, we found a cascade of rearrangements within the protein complex which manifest in three discrete time points of dynamic activity, conserved over hundreds of millions of years within a narrow window. Among these processes, one displays a subtle temporal shift correlating with evolutionary divergence, suggesting…
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Taxonomy
TopicsProtein Structure and Dynamics · Photosynthetic Processes and Mechanisms · Hemoglobin structure and function
