Machinery of Functional Dynamics in Native Proteins

TL;DR

This paper investigates the energy landscapes and dynamic regimes of native proteins, revealing how temperature influences their functional motions and identifying distinct backbone motion regimes linked to activity and pocket dynamics.

Contribution

It introduces a detailed analysis of the different dynamic regimes in protein energy landscapes and their relation to temperature and functional activity.

Findings

Energy landscapes of folded proteins do not shift with temperature.

Three distinct regimes of backbone motion are identified.

Active protein behavior emerges at specific temperature-induced pocket jumps.

Abstract

We provide evidence that the energy landscapes of folded proteins do not shift with temperature, but the onset of functional dynamics is associated with its effective sampling. The motion of the backbone is described by three distinct regimes. One is associated with slow time scales of the activity along the envelope of the energy surface defining the folded protein. Another, with fast time scales, is due to activity along the pockets decorating the folded-state envelope. The intermediate regime emerges at temperatures where jumps between the pockets become possible, leading to an active protein.