期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2020
卷号：117
期号：33
页码：19938-19942
DOI：10.1073/pnas.2008873117
出版社：The National Academy of Sciences of the United States of America
摘要：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 bioinformatic methods hitherto available.
