Resources
Proteomics Databases

Metabolomics Databases

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• Is Circular Dichroism Spectroscopy Accurate Before 250 Nanometers
When evaluating the precision and accuracy of spectroscopic measurements, several factors need to be considered, including the light source, detector, and the measurement methodology. Particularly in the ultraviolet region below 250 nanometers, technical limitations and inherent physical properties may pose challenges to achieving accurate spectra.
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• What Information About Peptides Can Be Directly Obtained From Mass Spectrometry Detection
Mass spectrometry is a crucial analytical technique used to determine the mass and structural composition of chemical substances. In biochemistry, it is particularly useful for peptide analysis, providing insights such as: 1. Peptide Mass: By measuring their mass-to-charge ratios, mass spectrometry can determine peptide masses and deduce their amino acid sequences. 2. Peptide Fragment Ions: Secondary mass spectrometry allows for the analysis of peptide fragments, facilitating the deduction of peptide.......
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• RNA Pull-Down Mass Spectrometry Analysis
RNA Pull Down is a widely used experimental method designed to investigate RNA-protein interactions. Mass spectrometry (MS) is a powerful and precise bioanalytical approach for identifying and characterizing the mass and sequence of proteins in complex biological samples. RNA Pull Down coupled with mass spectrometry integrates these two techniques, enabling the identification of proteins interacting with specific RNA molecules.
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• Can Protein Still Be Analyzed by Mass Spectrometry After Denaturation
Protein denaturation involves altering the protein's structure, converting it from a functional three-dimensional form into a non-functional one. Common denaturation methods include heating, and the addition of acids, bases, or organic solvents. Although denaturation changes the three-dimensional conformation, it typically does not affect the primary structure, the amino acid sequence. Therefore, mass spectrometry remains a viable method for identifying denatured proteins.
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• How Many Microliters Are Needed for Serum Mass Spectrometry Proteomics
In mass spectrometry-based proteomics studies, the sample volume significantly impacts the quality of the experimental results. For serum samples, the required volume depends on the analytical method employed and the sensitivity of the instrumentation. Typically, analyzing a serum sample requires between 20 and 100 microliters. Researchers should determine the exact volume needed based on their specific equipment and research objectives.
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• Cross-Linking Mass Spectrometry Sample Preparation
Cross-linking mass spectrometry (XL-MS) is a powerful analytical tool for elucidating protein structures and interactions, with the sample preparation process being a crucial determinant of experimental success. The preparation protocol for XL-MS encompasses four main stages: protein extraction, purification, cross-linking, and preparation of cross-linked protein samples for mass spectrometry analysis.
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• Translate Protein Interactions Using IPMax
Interacting proteins are defined as protein complexes formed through protein-protein interactions within cells, which are fundamental to key biological processes such as signal transduction, gene transcription and translation, and cell cycle regulation. IPMax leverages immunoprecipitation (IP), a widely used experimental technique for studying protein-protein interactions. This approach uses specific antibodies to isolate target proteins and their interacting partners, followed by protein mass spectrometry
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• Minimum Blood Volume for Proteomics Analysis
Blood proteomics provides valuable insights into the biological functions of blood and its roles in various pathological conditions. In studies of blood proteomics, there is no universally defined minimum volume for blood collection. The required sample volume is determined by the specific research objectives and the analytical techniques employed. Typically, a collection of approximately 1–2 milliliters of blood is considered adequate. The following factors influence the determination of the minimum.......
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COG (Clusters of Orthologous Groups of proteins) represents a systematic classification framework designed to categorize proteins in bacteria, archaea, and eukaryotes. COG analysis of protein profiles is primarily employed to assess the functional and evolutionary characteristics of protein sequences, grouping them into distinct categories based on orthology. The COG database is a comprehensive repository of protein profiles across multiple species, wherein protein sequences are grouped according to their..
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• Which Samples Can Be Submitted for High-Throughput Proteomics Analysis
Biological Fluid Samples These samples, which include blood, urine, cerebrospinal fluid, and saliva, contain proteins that serve as indicators of the body's health status. Tissue Samples Tissue samples encompass various human tissues such as liver, kidney, heart, lung, and brain, along with diverse tumor tissues. Analyzing proteins within these samples provides insights into tissue functionality and the underlying mechanisms of diseases.
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