Resources
Proteomics Databases
Metabolomics Databases

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• Analyzing Protein Secondary Structure Using Circular Dichroism Spectroscopy
Circular dichroism (CD) spectroscopy analysis has become an important tool in the field of biopharmaceutical analysis for studying protein secondary structure and providing critical information.
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• Effects of DMSO on Protein Structure
Dimethyl sulfoxide (DMSO), as one of the commonly used solvents, has a certain impact on protein structure.In circular dichroism spectroscopy, the choice of solvent is crucial in maintaining the integrity of protein structure.
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• Protein Characterization Revealing Protein Structure and Functions
Protein characterization is an important means to reveal the structure, interaction, and function of proteins. Through common protein structure identification techniques, we can deeply understand the working principle of proteins and apply this knowledge in fields such as biology, drug development, and bioengineering.
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• Diversity of Protein Glycosylation and Its Role in Biology
Protein glycosylation is a common and complex post-translational modification that adds sugar molecules to protein molecules. It regulates their structure, stability, and interactions, playing a crucial role in cellular function and biological processes. Protein glycosylation can be divided into two main types: N-glycosylation and O-glycosylation.
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• Assessing Drug Immunogenicity Through ADA Testing
As the use of antibody drugs increases, studies have found that some patients develop anti-drug antibodies (ADAs) after receiving treatment, which may have adverse effects on treatment efficacy and safety. Therefore, accurate assessment of drug immunogenicity has become a crucial task.
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• How to Choose the Appropriate Polysaccharide Mass Spectrometry Identification Technique?
Accurate polysaccharide mass spectrometry identification and structural analysis of polysaccharides are crucial steps in understanding their characteristics and functions.
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• Exploring Strategies for Quantitative Analysis of Disulfide Bonds in Proteins
Disulfide bonds are important chemical bonds in proteins and are crucial for protein structure and function. Quantitative analysis of disulfide bonds is a key step in understanding protein structure and function. However, due to the unique properties of disulfide bonds, their quantitative analysis has always been a challenge in the field of biopharmaceuticals.
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• Exploring Methods and Techniques for Protein Crosslinking Experiments
Protein crosslinking experiments are important methods for studying protein-protein interactions. By chemically or physically linking specific sites within proteins, these experiments reveal the interaction networks and complex structures of proteins.
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• Selection and Optimization of Protein Identification Methods
Protein identification is the process of identifying and analyzing proteins, including determining their sequence, structure, modifications, and functions. This article will introduce the significance and challenges of protein identification, and focus on the selection and optimization of protein identification methods.
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• Analyzing Protein Structure Using Circular Dichroism Spectroscopy
The basic principle of circular dichroism spectroscopy is a technique used to study the structure of molecules by measuring their absorption and rotation of circularly polarized light. Chiral amino acid residues in proteins produce optical rotation effects on circularly polarized light and exhibit specific absorption spectra. Circular dichroism spectroscopy obtains structural information of proteins by measuring the difference in absorption of left- and right-handed circularly polarized light.
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