Details

Autor(en) / Beteiligte

• Rackovsky, S.
• Scheraga, Harold A.

Titel

The structure of protein dynamic space

Ist Teil von

• Proceedings of the National Academy of Sciences - PNAS, 2020-08, Vol.117 (33), p.19938-19942

Ort / Verlag

United States: National Academy of Sciences

Erscheinungsjahr

2020

Quelle

MEDLINE

Beschreibungen/Notizen

• We use a bioinformatic description of amino acid dynamic properties, based on residue-specific average B factors, to construct a dynamics-based, large-scale description of a space of protein sequences. We examine the relationship between that space and an independently constructed, structure-based space comprising the same sequences. It is demonstrated that structure and dynamics are only moderately correlated. It is further shown that helical proteins fall into two classes with very different structure–dynamics relationships. We suggest that dynamics in the two helical classes are dominated by distinctly different modes—pseudo–one-dimensional, localized helical modes in one case, and pseudo–three-dimensional (3D) global modes in the other. Sheet/barrel and mixed-α/β proteins exhibit more conventional structure–dynamics relationships. It is found that the strongest correlation between structure and dynamic properties arises when the latter are represented by the sequence average of the dynamic index, which corresponds physically to the overall mobility of the protein. None of these results are accessible to bioinformaticmethods hitherto available.