Proteins are generally characterized by three-dimensional structures that are well suited for their specific function. It is much less accepted that a particular flexibility or plasticity of a protein is essential for performing its function. The latter plasticity encompasses the stochastic motions of small protein sidechains on the picosecond timescale that serve as “lubricating grease”, allowing slower functionally relevant conformational changes. Some remarkable examples of potential correlations between protein dynamics and function were observed for pigment–protein complexes in photosynthesis. For example, electron transfer and protein plasticity are concurrently suppressed in Photosystem II upon decreases in temperature or hydration, thus suggesting a prominent functional role of protein dynamics. An unusual dynamics–function correlation was observed for the major light-harvesting complex II, where the dynamics of charged protein residues affect the pigment absorption frequencies in photosynthetic light-harvesting. Generally, proteins exhibit a wide variety of motions on multiple time and length scales. However, there is an approach to characterize the plasticity of a protein as a single effective force constant that permits a straightforward comparison between different protein systems. Within this review, we determine the latter effective force constant for three photosynthetic proteins in different functional and organizational states. The force constant values determined appear to be rather different for each protein and are consistent with the requirements imposed by the various functions. These findings highlight the individual character of a protein’s flexibility and the role(s) it is playing for the specific function.
Koppel et al. (Mon,) studied this question.