Resources
Proteomics Databases
Metabolomics Databases
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• Confirming N-Glycosylation Sites via Mass Spectrometry
N-glycosylation is a key post-translational modification that affects protein folding, stability, and function. Identification of N-glycosylation sites is crucial for understanding protein structure and function, and mass spectrometry (MS) has become a critical tool in this field. The process typically involves the following steps.
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• Protein Sequencing Sample Requirements
Proteomics sequencing is a technique used to analyze protein expression, modifications, and interactions, often relying on mass spectrometry. In order to carry out effective proteomics analysis, sample preparation must meet certain requirements. Here are some common requirements for proteomics sequencing samples.
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• Does Mass Spectrometry Identify Specific Amino Acid Sequences?
Proteomics Mass Spectrometry refers to the use of mass spectrometry technology for the analysis of protein or peptide mass, in order to identify their amino acid sequence. In theory and in practice, mass spectrometry can provide specific amino acid sequence information of proteins or peptides. This is achieved by measuring the mass of the peptide and the fragments generated in the mass spectrometry.
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• Explore De Novo Protein Sequencing
De novo protein sequencing refers to a method of deriving the amino acid sequence of a protein or peptide directly from experimental data, without relying on known DNA or protein database information. It is particularly useful for studying proteins in species without a reference sequence or exploring new variants and modifications of proteins.
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• Recent Advances in N-Terminal Protein Sequencing
Protein N-terminal sequencing is the process of determining the amino acid sequence at the N-terminus of a protein or peptide chain. This is crucial for protein identification, analysis of signal peptide cleavage sites, and post-translational modification studies, among other areas. Recent advances in the field have been seen, particularly in the application of mass spectrometry and bioinformatics.
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• The Basic Processing Procedure of Protein Sequencing Sample
Protein sequencing typically refers to the determination of the precise order of amino acid residues in a protein molecule, which is a crucial step in understanding protein function and structure. The main technique used to achieve this is mass spectrometry analysis, particularly tandem mass spectrometry (MS/MS). The following are the basic processing steps for protein sequencing.
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• Protein Mutation Site Analysis
Mutation site analysis of proteins is an important biological research that focuses on specific changes that occur in the amino acid sequence of proteins, which may affect the function, stability, and/or interaction with other molecules of the protein. The following are basic concepts and methods of protein mutation site analysis.
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• Peptide Mass Spectrometry Result Interpretation Strategy
Mass spectrometry (MS), is an important technique for analyzing peptides or proteins. It determines the molecular weight and structure by measuring the mass-to-charge ratio (m/z) of the analyte ions. In proteomics, MS is commonly used for protein and peptide identification, as well as quantitative analysis. To interpret the mass spectrometry results for peptide analysis, it is necessary to have a basic understanding of the mass spectrum, including m/z (mass-to-charge ratio) and intensity.
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Protein motif analysis is an important task in bioinformatics, aiming to identify short sequence patterns in protein sequences that have specific functional or structural significance. These short sequences, often referred to as motifs or functional sites, are crucial for understanding the biological functions of proteins, protein-protein interactions, and regulatory mechanisms.
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• Methods and Applications for Protein Sequence Determination
Protein sequencing is the process of determining the exact order of amino acids in a protein. It can analyze amino acid sequences, confirm protein structure and function, identify new protein biomarkers and drug targets, construct phylogenetic trees to understand evolutionary relationships, and identify orthologous and paralogous proteins.
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