The dynamic basis of structural order in proteins

Area of Science:

• Biophysics
• Computational Biology
• Protein Science

Background:

• Proteins exist in folded or intrinsically disordered states (IDPs).
• Differences in amino acid composition between these states are empirically observed.
• The physical basis for these differences remains incompletely understood.

Purpose of the Study:

• To compare the sequence dynamics of folded proteins and IDPs.
• To investigate the role of long-length-scale dynamic properties in protein folding.
• To elucidate the physical basis for compositional differences between folded and disordered proteins.

Main Methods:

• Utilized recently developed bioinformatic methods.
• Analyzed protein sequences focusing on dynamic properties.
• Compared sequence organization and amino acid composition.

Main Results:

• Folded and IDP sequences exhibit diametrically opposite long-length-scale dynamic properties.
• A statistically significant difference in amino acid composition exists between folded and IDP sequences, reflected in their dynamics.
• Long-length-scale sequence properties are critical determinants of protein folding.

Conclusions:

• Protein folding is critically dependent on long-length-scale sequence dynamics.
• These dynamics provide a physical explanation for observed amino acid compositional differences.
• Understanding protein sequence dynamics is central to protein physics.