Resources

    Proteomics Databases

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    Metabolomics Databases

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  • • How to Achieve High-Throughput Quantification in Single Cell Proteomics? A Comprehensive Guide to TMT Labeling

    Cells are the fundamental units of biological processes; however, even genetically identical cells within the same environment can display substantial functional differences. Such intercellular heterogeneity is recognized as having critical biological significance in research fields including cancer, immunology, and developmental biology. In recent years, single cell RNA sequencing has advanced rapidly, and Tandem Mass Tag (TMT) labeling has emerged as a widely adopted core strategy for quantitative .......

  • • Protein Structure Identification: A Complete Guide from Sequence to Structure

    Proteins play central roles in cellular functions, and their structures provide the essential basis for functional realization. Understanding the three-dimensional architecture of proteins not only facilitates elucidation of their molecular mechanisms but also constitutes a critical prerequisite for target discovery, drug screening, and disease mechanism studies. With the rapid advancements in bioinformatics and structural biology, the prediction and identification of protein structures from amino acid ....

  • • What Exactly Is the Protein Primary Structure? Understanding the Importance of Amino Acid Sequence

    Proteins are fundamental biomolecules that execute a wide array of functions within cells. They participate in virtually all biological processes, including catalysis, signal transduction, structural support, molecular transport, and immune recognition. Despite the existence of thousands of protein species, all share a common essence: a polypeptide chain composed of the 20 standard amino acids arranged in a specific order. This arrangement constitutes the protein primary structure. In protein science, the..

  • • Circular Dichroism Spectroscopy Based Protein Secondary Structure Identification: Methods, Tools, and Pitfalls

    Protein structure dictates its function, with secondary structure serving as the fundamental element of the three-dimensional architecture. It plays a critical role in elucidating protein folding pathways, functional states, and interactions with ligands. Circular Dichroism (CD) spectroscopy, owing to its operational simplicity and minimal sample requirement, has been widely employed for the rapid characterization and dynamic monitoring of protein secondary structures. Principles of Circular Dichroism .....

  • • Principles and Experimental Design of Circular Dichroism (CD) Spectroscopy Analysis

    Circular Dichroism (CD) spectroscopy is a technique that measures the differential absorption of left- and right-circularly polarized light by chiral molecules. It is widely employed to investigate the conformational properties of biological macromolecules such as proteins and nucleic acids. This paper describes the fundamental principles of Circular Dichroism spectroscopy analysis, essential considerations in experimental design, and its significance in life science research. Overview of Circular ......

  • • Differences and Applications of Far-UV and Near-UV CD Spectroscopy in Protein Structure Research

    Circular Dichroism (CD) spectroscopy is a sensitive and non-destructive analytical technique widely employed in protein structure research. Depending on the measurement wavelength, CD spectra are categorized into far-ultraviolet (Far-UV, 190–250 nm) and near-ultraviolet (Near-UV, 250–320 nm) regions, each offering distinct advantages for probing different levels of protein structure. This paper systematically outlines the primary differences between these two CD techniques and highlights representative ....

  • • CD vs NMR vs X-ray: Which Structural Analysis Method is Right for You?

    In life sciences research and pharmaceutical development, the structural characterization of biological macromolecules plays a pivotal role. Among the most widely employed techniques are Circular Dichroism (CD), Nuclear Magnetic Resonance (NMR), and X-ray Crystallography, each offering distinct advantages suited to specific experimental contexts. This review outlines the selection criteria for these methods in terms of resolution, sample requirements, applicability, and experimental timeframe.

  • • How to Enhance Efficiency of Protein Structure Analysis Using Bioinformatics Tools?

    In contemporary life science research, protein structures serve as fundamental determinants for understanding the functional properties of biomolecules. Ranging from elucidating enzyme catalytic mechanisms and deciphering signaling pathway regulation to identifying drug targets, three-dimensional structural information offers irreplaceable biological insights. Protein structures define the spatial arrangement of amino acid residues within their three-dimensional conformations, forming the foundation for....

  • • How Can Protein Structure Analysis Facilitate Biopharmaceutical Development?

    In the rapidly evolving field of modern biopharmaceutical research and development, proteins, whether as primary therapeutic targets or as drug molecules, possess structural attributes that directly determine their biological functions and mechanisms of action. Protein structure analysis, as a central approach for elucidating protein molecular conformations, plays an indispensable role throughout the entire lifecycle of biopharmaceuticals, from discovery and design to optimization and quality control.

  • • Integrated Solutions for Protein Structure Identification and Functional Prediction

    In the post-genomic era, elucidating the three-dimensional structure and functional properties of proteins is a critical step toward advancing our understanding of biological processes. Proteins are fundamental functional units of cells, and the characterization of their structures and functions forms the essential basis for drug discovery, the investigation of disease mechanisms, and precision medicine. Classical structural biology techniques, such as X-ray crystallography, nuclear magnetic resonance .....

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