Qian-Yuan Tang 교수

Based on protein structural ensembles determined by nuclear magnetic resonance, we study the position fluctuations of residues by calculating distance-dependent correlations and conducting finite-size scaling analysis. The fluctuations exhibit high susceptibility and long-range correlations up to the protein sizes. The scaling relations between the correlations or susceptibility and protein sizes resemble those in other physical and biological systems near their critical points. These results in

The genotype-phenotype mapping of proteins is a fundamental question in structural biology. In this Letter, with the analysis of a large dataset of proteins from hundreds of protein families, we quantitatively demonstrate the correlations between the noise-induced protein dynamics and mutation-induced variations of native structures, indicating the dynamics-evolution correspondence of proteins. Based on the investigations of the linear responses of native proteins, the origin of such a correspon

Proteins in cellular environments are highly susceptible. Local perturbations to any residue can be sensed by other spatially distal residues in the protein molecule, showing long-range correlations in the native dynamics of proteins. The long-range correlations of proteins contribute to many biological processes such as allostery, catalysis, and transportation. Revealing the structural origin of such long-range correlations is of great significance in understanding the design principle of biolo

The recent development of artificial intelligence provides us with new and powerful tools for studying the mysterious relationship between organism evolution and protein evolution. In this work, based on the AlphaFold Protein Structure Database (AlphaFold DB), we perform comparative analyses of the proteins of different organisms. The statistics of AlphaFold-predicted structures show that, for organisms with higher complexity, their constituent proteins will have larger radii of gyration, higher

This paper studies the compatibility of the functional sensitivity and mutational robustness of proteins. The interplay of the two aspects leads to power-law distributions in the vibration spectra of proteins.

Abstract The recent development of artificial intelligence provides us with new and powerful tools for studying the mysterious relationship between organism evolution and protein evolution. In this work, based on the AlphaFold Protein Structure Database (AlphaFold DB), we perform comparative analyses of the proteins of different organisms. The statistics of AlphaFold-predicted structures show that, for organisms with higher complexity, their constituent proteins will have larger radii of gyratio

<strong>Abstract:</strong> The genotype-phenotype mapping of proteins is a fundamental question in structural biology. In this Letter, with the analysis of a large dataset of proteins from hundreds of protein families, we quantitatively demonstrate the correlations between the noise-induced protein dynamics and mutation-induced variations of native structures, indicating the dynamics-evolution correspondence of proteins. Based on the investigations of the linear responses of native proteins, the

The interplay between protein folding and native dynamics remains a central question in biophysics. Analyzing an extensive set of AlphaFold-predicted structures, we uncover a robust relationship between folding topology (contact order) and native dynamics (fluctuation entropy), showing that long-range contacts that slow folding also restrict conformational flexibility across protein sizes and taxonomic groups. Scaling analysis reveals that this relationship, together with its chain-length depend

データ駆動型解析により，タンパク質のダイナミクスと進化に共通する特徴の物理的起源が明らかになり，頑健性と可塑性のトレードオフが示された．さらに，AlphaFoldによって予測されたタンパク質構造データベースを基に，タンパク質進化の統計的傾向を分析し，進化的次元削減を実証し，生物学的複雑性の普遍的法則を強調した．

<strong>Abstract:</strong> The genotype-phenotype mapping of proteins is a fundamental question in structural biology. In this Letter, with the analysis of a large dataset of proteins from hundreds of protein families, we quantitatively demonstrate the correlations between the noise-induced protein dynamics and mutation-induced variations of native structures, indicating the dynamics-evolution correspondence of proteins. Based on the investigations of the linear responses of native proteins, the

Sensitivity and robustness appear to be contrasting concepts. However, natural proteins are robust enough to tolerate random mutations, meanwhile be susceptible enough to sense environmental signals, exhibiting both high functional sensitivity (i.e., plasticity) and mutational robustness. Uncovering how these two aspects are compatible is a fundamental question in the protein dynamics and genotype-phenotype relation. In this work, a general framework is established to analyze the dynamics of pro

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