Physics of Proteins at Low Temperature

TL;DR

This study investigates the low-temperature dynamics of proteins using spectral diffusion experiments, revealing characteristic features linked to protein organization, randomness, and finite size effects.

Contribution

It introduces experimental insights into protein behavior at low temperatures, highlighting the roles of organization, randomness, and finite size in spectral diffusion patterns.

Findings

Characteristic spectral diffusion features for protein states

Influence of organization and randomness on dynamics

Finite size effects impact low-temperature behavior

Abstract

We present results of a hole burning study with thermal cycling and waiting time spectral diffusion experiments on a modified cytochrome - c protein in its native as well as in its denatured state. The experiments show features which seem to be characteristic for the protein state of matter and its associated dynamics at low temperature. The properties responsible for the observed patterns are organisation paired with randomness and, in addition, the finite size which gives rise to surface and solvent effects. We discuss some general model approaches which might serve as guide lines for understanding these features.