Resources

Proteomics Databases



Metabolomics Databases

• • Mechanism of Histone Post-Translational Modification Analysis

  Histones are essential components of chromatin, playing critical roles in various biological processes such as gene expression regulation, DNA repair, and chromosome segregation by controlling DNA accessibility. The function of histones is not solely determined by their primary amino acid sequences but is significantly influenced by post-translational modifications (PTMs), such as acetylation, methylation, phosphorylation, and ubiquitination.

• • Workflow of Histone Post-Translational Modification Analysis

  Histones are key components of chromatin, playing a crucial role in DNA packaging into nucleosomes and regulating gene expression. Post-translational modifications (PTMs) of histones refer to the addition of various chemical groups to amino acid residues of histones by specific enzymes after protein synthesis. These modifications alter the physicochemical properties of histones, impacting chromatin structure and gene transcription activity.

• • Application of Histone Post-Translational Modification Analysis

  Histone post-translational modifications (PTMs) refer to chemical changes that occur in histones after protein synthesis. These modifications include acetylation, methylation, phosphorylation, and ubiquitination, among others. They not only affect the dynamic regulation of chromatin structure but also play a critical role in controlling gene expression. As a key mechanism in epigenetics, histone PTMs are essential for regulating gene activity and cellular function.

• • Advantages and Disadvantages of Histone Post-Translational Modification Analysis

  Histones are crucial components of chromatin structure and gene expression regulation. They are involved in numerous cellular biological processes through post-translational modifications (PTMs), including acetylation, methylation, phosphorylation, and ubiquitination. These modifications regulate gene expression levels by influencing chromatin conformation and interactions with transcription factors.

• • Principle of Histone Post-Translational Modification Analysis

  Histones are highly conserved basic proteins that play a crucial role in the formation of chromatin structure and the regulation of gene expression in eukaryotes. By binding to DNA, histones form nucleosomes, structures that not only compact DNA but also regulate processes such as gene expression, DNA repair, and replication. However, histones are not static molecules. Their functions and dynamic properties are partially regulated by post-translational modifications (PTMs).

• • Mechanism of Disulfide Bond Identification in Protein Analysis

  Proteins, as one of the most important biomolecules in living organisms, have structures and functions that are closely related to their three-dimensional conformations. The folding and stability of these conformations are regulated by various covalent and non-covalent interactions, among which disulfide bonds (S-S bonds) play a critical role. Disulfide bond formation is crucial for the folding, structural stability, and functional regulation of proteins, especially in secreted and membrane-bound proteins.

• • Application of Disulfide Bond Analysis in Proteomics

  Proteins are essential molecules that perform nearly all cellular functions within living organisms. Disulfide bonds, a crucial covalent modification within proteins, play significant roles in protein folding, stability, and function. They are also involved in cellular signaling and enzyme activity regulation. With advancements in proteomics, disulfide bond analysis has emerged as a key area for studying the relationship between protein structure and function.

• • Workflow of Protein Disulfide Bond Detection

  Protein disulfide bonds are crucial chemical bonds that maintain the tertiary and quaternary structures of proteins, playing key roles in redox reactions. Detecting and analyzing these bonds is essential for understanding protein structure and function, elucidating disease mechanisms, and developing novel therapeutics.

• • Advantages and Disadvantages of Disulfide Bond Mapping

  Disulfide bonds are critical covalent linkages in proteins that play essential roles in maintaining their three-dimensional structure, stability, and function. Disulfide bond mapping is a technique used to determine the patterns of disulfide linkages in proteins, providing insights into protein folding, structure, and stability. This technique is widely utilized in structural biology, drug development, and protein engineering.

• • Principle of Protein Disulfide Bond Quantification

  Protein disulfide bonds, formed through the oxidation of thiol groups (-SH) of two cysteine residues, are covalent linkages that play a pivotal role in stabilizing the tertiary and quaternary structures of proteins. The dynamic formation and reduction of these bonds are critical for protein folding, structural integrity, and functional modulation, and are implicated in the pathogenesis of various diseases.