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Kleeorin, Y.

Publications and source records attributed to Kleeorin, Y..

2 recordsLinked to original sources

Improved inference of multiscale sequence statistics in generative protein models

High dimensionality and multiscale statistical structure are pervasive features of biological data, posing fundamental challenges for modeling. Because model inference generally proceeds with far fewer data than parameters, statistical patterns across scales are often unevenly represented. Protein sequences provide a paradigmatic example: statistics across homologs are inherently multiscale, displaying collective correlations among conserved residue sectors that encode function, alongside localized correlations corresponding to physical contacts outside these sectors. Standard regularization strategies used to mitigate undersampling during model inference have been shown to capture these patterns unevenly, a bias that compromises generative models of protein sequences by limiting their ability to produce both functional and diverse proteins. This limitation is exemplified by Boltzmann Machine-based generative models, which so far have required post hoc corrections to recover functionality, at the cost of reduced sequence diversity and novelty. Here, we introduce the stochastic Boltzmann Machine (sBM), a new regularization strategy that more accurately captures different correlation scales. Through analyses of theoretical models with known ground-truth parameters and experiments on the chorismate mutase family, we show that sBM effectively mitigates distortions in the estimation of model parameters, enabling the generation of functional sequences with greater diversity and without the need for post hoc corrections. These results advance the inference of generative models that more faithfully reflect the evolutionary constraints shaping protein sequences.

systems biology↗

Undersampling and the inference of coevolution in proteins

Protein structure, function, and evolution depend on local and collective epistatic interactions between amino acids. A powerful approach to defining these interactions is to construct models of couplings between amino acids that reproduce the empirical statistics (frequencies and correlations) observed in sequences comprising a protein family. The top couplings are then interpreted. Here, we show that as currently implemented, this inference is always biased, a problem that fundamentally arises from the distinct scales at which epistasis occurs in proteins in the context of limited sampling. We show that these issues explain the ability of current approaches to predict tertiary contacts between amino acids and the inability to obviously expose larger networks of functionally-relevant, collectively evolving residues called sectors. This work provides a necessary foundation for more deeply understanding and improving evolution-based models of proteins.

biophysics↗