Comparing proteins by their internal dynamics: exploring structure-function relationships beyond static structural alignments

TL;DR

This paper reviews recent progress in comparing proteins based on their internal dynamics, emphasizing how dynamic features can reveal functional and evolutionary relationships beyond static structural alignments.

Contribution

It highlights the development of methods for dynamics-based protein comparison, advancing understanding of structure-function relationships beyond traditional approaches.

Findings

Dynamics-based comparisons can detect elusive protein relationships.

Protein flexibility and dynamics are evolutionarily conserved.

Methods improve understanding of structure-function relationships.

Abstract

The growing interest for comparing protein internal dynamics owes much to the realization that protein function can be accompanied or assisted by structural fluctuations and conformational changes. Analogously to the case of functional structural elements, those aspects of protein flexibility and dynamics that are functionally oriented should be subject to evolutionary conservation. Accordingly, dynamics-based protein comparisons or alignments could be used to detect protein relationships that are more elusive to sequence and structural alignments. Here we provide an account of the progress that has been made in recent years towards developing and applying general methods for comparing proteins in terms of their internal dynamics and advance the understanding of the structure-function relationship.