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Xiaoliang Ma

Publications and source records attributed to Xiaoliang Ma.

11 recordsLinked to original sources

A Semiparametric Framework for Stochastic Fundamental Diagram Modeling

The stochastic fundamental diagram (SFD) provides a probabilistic description of the relationship between traffic density and flow or speed, enabling uncertainty-aware traffic modeling. However, existing stochastic models frequently struggle to accommodate rigorous physical constraints while retaining sufficient flexibility to capture complex nonlinear patterns. To address this, we propose a novel semiparametric SFD modeling framework by leveraging specially designed functional forms. These functions intrinsically satisfy physical constraints defined on the moments of the conditional flow distribution given traffic density while incorporating neural-network-based structures to capture complex empirical patterns. We derive a system of moment-matching equations to convert physical constraints into the parameterization of the conditional distribution, proving that a unique solution exists for the location-scale family of distributions, thereby guaranteeing model well-posedness. Furthermore, we demonstrate that the framework can be extended to non-location-scale distributions, including those requiring additional boundary constraints. Empirical evaluations on a real-world dataset reveal that our approach consistently outperforms representative baselines, delivering superior probabilistic accuracy and robust uncertainty quantification, particularly in congested regimes. Overall, the proposed framework provides a theoretically grounded and flexible foundation for stochastic traffic flow modeling.

cs.LG

Graph-based Semantic Calibration Network for Unaligned UAV RGBT Image Semantic Segmentation and A Large-scale Benchmark

Fine-grained RGBT image semantic segmentation is crucial for all-weather unmanned aerial vehicle (UAV) scene understanding. However, UAV RGBT image semantic segmentation faces two coupled challenges: cross-modal spatial misalignment caused by sensor parallax and platform vibration, and severe semantic confusion among fine-grained ground objects under top-down aerial views. To address these issues, we propose a Graph-based Semantic Calibration Network (GSCNet) for unaligned UAV RGBT image semantic segmentation. Specifically, we design a Feature Decoupling and Alignment Module (FDAM) that decouples each modality into shared structural and private perceptual components and performs deformable alignment in the shared subspace, enabling robust spatial correction with reduced modality appearance interference. Moreover, we propose a Semantic Graph Calibration Module (SGCM) that explicitly encodes the hierarchical taxonomy and co-occurrence regularities among ground-object categories in UAV scenes into a structured category graph, and incorporates these priors into graph-attention reasoning to calibrate predictions of visually similar and rare categories. In addition, we construct the Unaligned RGB-Thermal Fine-grained (URTF) benchmark, to the best of our knowledge, the largest and most fine-grained benchmark for unaligned UAV RGBT image semantic segmentation, containing over 25,000 image pairs across 61 semantic categories with realistic cross-modal misalignment. Extensive experiments on URTF demonstrate that GSCNet significantly outperforms state-of-the-art methods, with notable gains on fine-grained categories. The dataset is available at https://github.com/mmic-lcl/Datasets-and-benchmark-code.

cs.CV

Interpretable Air Pollution Forecasting by Physics-Guided Spatiotemporal Decoupling

Accurate and interpretable air pollution forecasting is crucial for public health, but most models face a trade-off between performance and interpretability. This study proposes a physics-guided, interpretable-by-design spatiotemporal learning framework. The model decomposes the spatiotemporal behavior of air pollutant concentrations into two transparent, additive modules. The first is a physics-guided transport kernel with directed weights conditioned on wind and geography (advection). The second is an explainable attention mechanism that learns local responses and attributes future concentrations to specific historical lags and exogenous drivers. Evaluated on a comprehensive dataset from the Stockholm region, our model consistently outperforms state-of-the-art baselines across multiple forecasting horizons. Our model's integration of high predictive performance and spatiotemporal interpretability provides a more reliable foundation for operational air-quality management in real-world applications.

cs.LG

Text-Guided Coarse-to-Fine Fusion Network for Robust Remote Sensing Visual Question Answering

Remote Sensing Visual Question Answering (RSVQA) has gained significant research interest. However, current RSVQA methods are limited by the imaging mechanisms of optical sensors, particularly under challenging conditions such as cloud-covered and low-light scenarios. Given the all-time and all-weather imaging capabilities of Synthetic Aperture Radar (SAR), it is crucial to investigate the integration of optical-SAR images to improve RSVQA performance. In this work, we propose a Text-guided Coarse-to-Fine Fusion Network (TGFNet), which leverages the semantic relationships between question text and multi-source images to guide the network toward complementary fusion at the feature level. Specifically, we develop a Text-guided Coarse-to-Fine Attention Refinement (CFAR) module to focus on key areas related to the question in complex remote sensing images. This module progressively directs attention from broad areas to finer details through key region routing, enhancing the model's ability to focus on relevant regions. Furthermore, we propose an Adaptive Multi-Expert Fusion (AMEF) module that dynamically integrates different experts, enabling the adaptive fusion of optical and SAR features. In addition, we create the first large-scale benchmark dataset for evaluating optical-SAR RSVQA methods, comprising 6,008 well-aligned optical-SAR image pairs and 1,036,694 well-labeled question-answer pairs across 16 diverse question types, including complex relational reasoning questions. Extensive experiments on the proposed dataset demonstrate that our TGFNet effectively integrates complementary information between optical and SAR images, significantly improving the model's performance in challenging scenarios. The dataset is available at: https://github.com/mmic-lcl/. Index Terms: Remote Sensing Visual Question Answering, Multi-source Data Fusion, Multimodal, Remote Sensing, OPT-SAR.

cs.CV

Physics-data-driven intelligent optimization for large-scale meta-devices

Meta-devices have gained significant attention and have been widely utilized in optical systems for focusing and imaging, owing to their lightweight, high-integration, and exceptional-flexibility capabilities. However, based on the assumption of local phase approximation, traditional design method neglect the local lattice coupling effect between adjacent meta-atoms, thus harming the practical performance of meta-devices. Using physics-driven or data-driven optimization algorithms can effectively solve the aforementioned problems. Nevertheless, both of the methods either involve considerable time costs or require a substantial amount of data sets. Here, we propose a physics-data-driven approach based "intelligent optimizer" that enables us to adaptively modify the sizes of the studied meta-atom according to the sizes of its surrounding ones. Such a scheme allows to mitigate the undesired local lattice coupling effect, and the proposed network model works well on thousands of datasets with a validation loss of 3*10-3. Experimental results show that the 1-mm-diameter metalens designed with the "intelligent optimizer" possesses a relative focusing efficiency of 93.4% (as compared to ideal focusing) and a Strehl ratio of 0.94. In contrast to the previous inverse design method, our method significantly boosts designing efficiency with five orders of magnitude reduction in time. Our design approach may sets a new paradigm for devising large-scale meta-devices.

physics.optics

The low-entropy hydration shell at the binding site of spike RBD determines the contagiousness of SARS-CoV-2 variants

The infectivity of SARS-CoV-2 depends on the binding affinity of the receptor-binding domain (RBD) of the spike protein with the angiotensin converting enzyme 2 (ACE2) receptor. The calculated RBD-ACE2 binding energies indicate that the difference in transmission efficiency of SARS-CoV-2 variants cannot be fully explained by electrostatic interactions, hydrogen-bond interactions, van der Waals interactions, internal energy, and nonpolar solvation energies. Here, we demonstrate that low-entropy regions of hydration shells around proteins drive hydrophobic attraction between shape-matched low-entropy regions of the hydration shells, which essentially coordinates protein-protein binding in rotational-configurational space of mutual orientations and determines the binding affinity. An innovative method was used to identify the low-entropy regions of the hydration shells of the RBDs of multiple SARS-CoV-2 variants and the ACE2. We observed integral low-entropy regions of hydration shells covering the binding sites of the RBDs and matching in shape to the low-entropy region of hydration shell at the binding site of the ACE2. The RBD-ACE2 binding is thus found to be guided by hydrophobic collapse between the shape-matched low-entropy regions of the hydration shells. A measure of the low-entropy of the hydration shells can be obtained by counting the number of hydrophilic groups expressing hydrophilicity within the binding sites. The low-entropy level of hydration shells at the binding site of a spike protein is found to be an important indicator of the contagiousness of the coronavirus.

q-bio.BM

Space Layout of Low-entropy Hydration Shells Guides Protein Binding

Protein-protein binding enables orderly and lawful biological self-organization, and is therefore considered a miracle of nature. Protein-protein binding is steered by electrostatic forces, hydrogen bonding, van der Waals force, and hydrophobic interactions. Among these physical forces, only the hydrophobic interactions can be considered as long-range intermolecular attractions between proteins in intracellular and extracellular fluid. Low-entropy regions of hydration shells around proteins drive hydrophobic attraction among them that essentially coordinate protein-protein docking in rotational-conformational space of mutual orientations at the guidance stage of the binding. Here, an innovative method was developed for identifying the low-entropy regions of hydration shells of given proteins, and we discovered that the largest low-entropy regions of hydration shells on proteins typically cover the binding sites. According to an analysis of determined protein complex structures, shape matching between the largest low-entropy hydration shell region of a protein and that of its partner at the binding sites is revealed as a regular pattern. Protein-protein binding is thus found to be mainly guided by hydrophobic collapse between the shape-matched low-entropy hydration shells that is verified by bioinformatics analyses of hundreds of structures of protein complexes. A simple algorithm is developed to precisely predict protein binding sites.

q-bio.BM

Hydrophobic interaction determines docking affinity of SARS CoV 2 variants with antibodies

Preliminary epidemiologic, phylogenetic and clinical findings suggest that several novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants have increased transmissibility and decreased efficacy of several existing vaccines. Four mutations in the receptor-binding domain (RBD) of the spike protein that are reported to contribute to increased transmission. Understanding physical mechanism responsible for the affinity enhancement between the SARS-CoV-2 variants and ACE2 is the "urgent challenge" for developing blockers, vaccines and therapeutic antibodies against the coronavirus disease 2019 (COVID-19) pandemic. Based on a hydrophobic-interaction-based protein docking mechanism, this study reveals that the mutation N501Y obviously increased the hydrophobic attraction and decrease hydrophilic repulsion between the RBD and ACE2 that most likely caused the transmissibility increment of the variants. By analyzing the mutation-induced hydrophobic surface changes in the attraction and repulsion at the binding site of the complexes of the SARS-CoV-2 variants and antibodies, we found out that all the mutations of N501Y, E484K, K417N and L452R can selectively decrease or increase their binding affinity with some antibodies.

q-bio.BM

The role of hydrophobic interactions in folding of $β$-sheets

Exploring the protein-folding problem has been a long-standing challenge in molecular biology. Protein folding is highly dependent on folding of secondary structures as the way to pave a native folding pathway. Here, we demonstrate that a feature of a large hydrophobic surface area covering most side-chains on one side or the other side of adjacent $β$-strands of a $β$-sheet is prevail in almost all experimentally determined $β$-sheets, indicating that folding of $β$-sheets is most likely triggered by multistage hydrophobic interactions among neighbored side-chains of unfolded polypeptides, enable $β$-sheets fold reproducibly following explicit physical folding codes in aqueous environments. $β$-turns often contain five types of residues characterized with relatively small exposed hydrophobic proportions of their side-chains, that is explained as these residues can block hydrophobic effect among neighbored side-chains in sequence. Temperature dependence of the folding of $β$-sheet is thus attributed to temperature dependence of the strength of the hydrophobicity. The hydrophobic-effect-based mechanism responsible for $β$-sheets folding is verified by bioinformatics analyses of thousands of results available from experiments. The folding codes in amino acid sequence that dictate formation of a $β$-hairpin can be deciphered through evaluating hydrophobic interaction among side-chains of an unfolded polypeptide from a $β$-strand-like thermodynamic metastable state.

q-bio.BM

A hydrophobic-interaction-based mechanism trigger docking between the SARS CoV 2 spike and angiotensin-converting enzyme 2

A recent experimental study found that the binding affinity between the cellular receptor human angiotensin converting enzyme 2 (ACE2) and receptor-binding domain (RBD) in spike (S) protein of novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is more than 10-fold higher than that of the original severe acute respiratory syndrome coronavirus (SARS-CoV). However, main-chain structures of the SARS-CoV-2 RBD are almost the same with that of the SARS-CoV RBD. Understanding physical mechanism responsible for the outstanding affinity between the SARS-CoV-2 S and ACE2 is the "urgent challenge" for developing blockers, vaccines and therapeutic antibodies against the coronavirus disease 2019 (COVID-19) pandemic. Considering the mechanisms of hydrophobic interaction, hydration shell, surface tension, and the shielding effect of water molecules, this study reveals a hydrophobic-interaction-based mechanism by means of which SARS-CoV-2 S and ACE2 bind together in an aqueous environment. The hydrophobic interaction between the SARS-CoV-2 S and ACE2 protein is found to be significantly greater than that between SARS-CoV S and ACE2. At the docking site, the hydrophobic portions of the hydrophilic side chains of SARS-CoV-2 S are found to be involved in the hydrophobic interaction between SARS-CoV-2 S and ACE2. We propose a method to design live attenuated viruses by mutating several key amino acid residues of the spike protein to decrease the hydrophobic surface areas at the docking site. Mutation of a small amount of residues can greatly reduce the hydrophobic binding of the coronavirus to the receptor, which may be significant reduce infectivity and transmissibility of the virus.

q-bio.BM

Physical Folding Codes for Proteins

Exploring and understanding the protein-folding problem has been a long-standing challenge in molecular biology. Here, using molecular dynamics simulation, we reveal how parallel distributed adjacent planar peptide groups of unfolded proteins fold reproducibly following explicit physical folding codes in aqueous environments due to electrostatic attractions. Superfast folding of protein is found to be powered by the contribution of the formation of hydrogen bonds. Temperature-induced torsional waves propagating along unfolded proteins break the parallel distributed state of specific amino acids, inferred as the beginning of folding. Electric charge and rotational resistance differences among neighboring side-chains are used to decipher the physical folding codes by means of which precise secondary structures develop. We present a powerful method of decoding amino acid sequences to predict native structures of proteins. The method is verified by comparing the results available from experiments in the literature.

q-bio.BM