Temperature dependence of normal mode reconstructions of protein dynamics

TL;DR

This study examines how normal mode analysis can effectively reconstruct protein dynamics across various temperatures, emphasizing the importance of multiple modes for accurate modeling at physiological conditions.

Contribution

It demonstrates the temperature-dependent reliability of normal mode analysis and highlights the necessity of multiple modes to accurately capture protein fluctuations.

Findings

Normal modes are valid for protein dynamics near physiological temperatures.

Single-mode contributions vary unpredictably with temperature.

Using multiple modes improves the accuracy of protein fluctuation reconstructions.

Abstract

Normal mode analysis is a widely used technique for reconstructing conformational changes of proteins from the knowledge of native structures. In this Letter, we investigate to what extent normal modes capture the salient features of the dynamics over a range of temperatures from close to T = 0 to above unfolding. We show that on the one hand, the use of normal modes at physiological temperatures is justified provided proteins are cooperative. On the other hand, it is imperative to consider several modes in order to eliminate the unpredictable temperature dependence of single- mode contributions to the protein fluctuations.