Wavelet-Enhanced Data-Driven Collective Variables for Efficient Sampling of Protein Folding Landscapes

The development of collective variables (CVs) capable of distinguishing important (meta)stable states and describing slow degrees of freedom (DOFs) is widely recognized as a prerequisite for the success of CV-based enhanced sampling methods, particularly in biomolecular systems where the underlying free-energy landscapes are extremely complex. For complex biochemical processes, selecting suitable geometric CVs for enhanced sampling often relies on chemical intuition, which is challenging and system-dependent. While data-driven CVs have emerged as a promising approach and achieved significant success in recent years, studies indicate that their performance is highly susceptible to fast stochastic fluctuations in molecular simulation trajectories, thereby obscuring the identification of slow DOFs. To overcome this limitation, we turn to a feature extraction strategy that utilizes the discrete wavelet transform to filter out fast-mode motions from MD trajectories, followed by dimensionality reduction of the descriptors. This refined feature subset provides an optimal input for constructing data-driven low-dimensional CVs, allowing for the identification of biologically relevant slow modes with high fidelity. We validate the efficacy of this strategy through a comparative analysis of chignolin and further showcase its applicability to the structurally more complex BBA protein system, which features both helical and antiparallel β-sheet motifs. The results reveal that the CVs derived from this strategy facilitate rapid transitions between folded and unfolded states, thereby significantly accelerating the exploration of protein folding landscapes across systems of varying scales.

Authors

Institutions

Publication Details

Journal
Journal of Chemical Information and Modeling
Published
2026-04-02
DOI
https://doi.org/10.1021/acs.jcim.6c00310
Primary Topic
Protein Structure and Dynamics
Type
article
Field-Weighted Citation Impact
0.00

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Wavelet-Enhanced Data-Driven Collective Variables for Efficient Sampling of Protein Folding Landscapes

Z Y Zhang, Xueguang Shao, Wensheng Cai
Journal of Chemical Information and Modeling
Protein Structure and Dynamics
article

Wavelet-Enhanced Data-Driven Collective Variables for Efficient Sampling of Protein Folding Landscapes

Z Y Zhang, Xueguang Shao, Wensheng Cai
article en

Abstract

The development of collective variables (CVs) capable of distinguishing important (meta)stable states and describing slow degrees of freedom (DOFs) is widely recognized as a prerequisite for the success of CV-based enhanced sampling methods, particularly in biomolecular systems where the underlying free-energy landscapes are extremely complex. For complex biochemical processes, selecting suitable geometric CVs for enhanced sampling often relies on chemical intuition, which is challenging and system-dependent. While data-driven CVs have emerged as a promising approach and achieved significant success in recent years, studies indicate that their performance is highly susceptible to fast stochastic fluctuations in molecular simulation trajectories, thereby obscuring the identification of slow DOFs. To overcome this limitation, we turn to a feature extraction strategy that utilizes the discrete wavelet transform to filter out fast-mode motions from MD trajectories, followed by dimensionality reduction of the descriptors. This refined feature subset provides an optimal input for constructing data-driven low-dimensional CVs, allowing for the identification of biologically relevant slow modes with high fidelity. We validate the efficacy of this strategy through a comparative analysis of chignolin and further showcase its applicability to the structurally more complex BBA protein system, which features both helical and antiparallel β-sheet motifs. The results reveal that the CVs derived from this strategy facilitate rapid transitions between folded and unfolded states, thereby significantly accelerating the exploration of protein folding landscapes across systems of varying scales.

Journal of Chemical Information and ModelingVol. 66(8)
Nankai University (CN), Unité Matériaux et Transformations (FR)
National Natural Science Foundation of China
Openalex Percentile: Top 32%
Protein Structure and Dynamics
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.