# The Spatial Distribution of Local Mobility in Folded Proteins

## TL;DR

This paper introduces a method to study how amino acid mobility is distributed in proteins, revealing that mobility patterns may influence protein dynamics and evolution.

## Contribution

A new method to analyze spatial mobility distribution in proteins using bioinformatics and signal processing tools.

## Key findings

- Mobility is nonuniformly distributed in a significant subset of protein structures.
- Nonuniform mobility distribution is not linked to specific protein fold classes.
- Differences in local mobility correlate with differences in total mobility.

## Abstract

A quantitative approach
is developed to the study of the spatial
distribution of amino acid mobility in protein structures. This method,
which is based on bioinformatic and signal processing tools, makes
it possible to study very large databases of structures simultaneously,
and to search for the existence of domains within proteins which are
defined by mobility effects, rather than by static structural considerations.
It is shown that mobility is distributed nonuniformly in a substantial
subset of structures in a large database; that nonuniform mobility
distribution does not select for fold class; and that differences
in local mobility distribution are correlated with differences in
total mobility. Analyzed in light of previous results, these findings
suggest that the dynamics of proteins with nonuniform distributions
of mobility may exhibit dynamics dominated by local modes, rather
than large-scale motions. We suggest that spatial mobility distribution
may be a significant driver of protein evolution. It is also speculated
that mobility distribution may act as a control on the hydrodynamic
environment of proteins in solution.