ArticleThe journal of physical chemistry. B2023
Functional Protein Dynamics Directly from Sequences.
Article in The journal of physical chemistry. B, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- MODEL-FREE INFERENCE FOR CHARACTERIZING PROTEIN MUTATIONS THROUGH A COEVOLUTIONARY LENS.The annals of applied statistics · 2026Article
- Major advances in protein function assignment by remote homolog detection with protein language models - A review.Current opinion in structural biology · 2025Review
- Machine Learning-Guided Protein Engineering.ACS catalysis · 2023Review
- In Silico Structural Analysis Exploring Conformational Folding of Protein Variants in Alzheimer's Disease.International journal of molecular sciences · 2023Article
- New alignment method for remote protein sequences by the direct use of pairwise sequence correlations and substitutions.Frontiers in bioinformatics · 2023Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The sequence correlations within a protein multiple sequence alignment are routinely being used to predict contacts within its structure, but here we point out that these data can also be used to predict a protein's dynamics directly. The elastic network protein dynamics models rely directly upon the contacts, and the normal modes of motion are obtained from the decomposition of the inverse of the contact map. To make the direct connection between sequence and dynamics, it is necessary to apply coarse-graining to the structure at the level of one point per amino acid, which has often been done, and protein coarse-grained dynamics from elastic network models has been highly successful, particularly in representing the large-scale motions of proteins that usually relate closely to their functions. The interesting implication of this is that it is not necessary to know the structure itself to obtain its dynamics and instead to use the sequence information directly to obtain the dynamics.
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Registered trials
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