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• • What Are the Applications of Circular Dichroism in Protein Research

  Circular dichroism (CD) leverages the optical rotation occurring when circularly polarized light interacts with chiral molecules to study their structures. As circularly polarized light passes through these molecules, the direction of light rotation changes—a phenomenon called optical rotation. CD measures differences in light absorption to produce signals that reveal structural characteristics of the sample.   1. Protein Structure Analysis CD provides insights into the secondary structures of protein......

• • The Secrets to Biomolecular Composition: What Does Circular Dichroism Spectroscopy Reveal

  Biomolecules are the essential building blocks of life, yet deciphering their structure and composition remains challenging. Circular dichroism (CD) spectroscopy allows researchers to study molecular structures by measuring how molecules absorb circularly polarized light. By examining CD spectra, scientists can gain detailed insights into the secondary structures, chiral properties, and stereochemistry of biomolecules, which provides valuable clues for understanding their functions and interactions.  ......

• • How to Measure the Extinction Coefficient?

  The extinction coefficient refers to a substance's ability to absorb light at a given concentration. It is related to the molar absorptivity of the substance and the path length. The molar absorptivity indicates the substance's ability to absorb light at a unit molar concentration, while the path length represents the distance light travels through the solution. The extinction coefficient can be calculated as the product of the molar absorptivity and path length. In the field of biopharmaceutical anal......

• • De Novo Sequencing Sample Quantity

  De novo sequencing, also known as sequencing from scratch, is a method used for sequence analysis of proteins or peptides, particularly suitable for analysis in the absence or incompleteness of reference sequences. This technique primarily relies on mass spectrometry (MS) data to infer the original sequence of proteins or peptides by analyzing the mass spectra fragmentation patterns of peptide ions.

• • The Use of Mass Spectrometry in Protein Identification Processes

  Mass spectrometry (MS) is a powerful and precise tool for the identification of proteins in biological and biochemical research. It allows researchers to identify proteins and their modifications in complex biological samples. The basic steps for protein identification using mass spectrometry are as follows.

• • Analysis of 3' Poly(A) Tail in Human Cell mRNA

  The mRNA (messenger ribonucleic acid) in human cells is a crucial intermediate product for gene expression, carrying genetic information from DNA transcription to protein translation. The maturation and stability of mRNA are regulated through a series of post-transcriptional modifications, with one of the most important processes being the addition of a poly(A) tail at the 3' end.

• • The Application of CD in Protein Secondary Structure Analysis

  Circular Dichroism (CD) is a widely used technique for analyzing protein secondary structure. It is based on the differential absorption of polarized light by different protein secondary structures, providing information about protein conformation. In protein secondary structure analysis, the applications of CD spectroscopy mainly include the following aspects.

• • Principle of Salivary Acid Detection for Cell Membrane

  Sialic acid is a type of terminal sugar residue widely present on glycoproteins and glycolipids on the cell membrane surface of animals, and it plays important biological roles. The principle of sialic acid detection on the cell membrane is based on the specific binding of certain molecules (such as lectins or antibodies) to cell surface sialic acid, followed by observation and analysis of this binding using appropriate detection methods.

• • Overview of Antibody Drug Thermal Stability Analysis Services

  Thermal stability analysis of antibody drugs is a crucial step to ensure drug quality, safety, and efficacy. Thermal stability studies involve exposing antibody drugs to different temperature conditions and subsequently assessing changes in their structure, function, and biological activity.

• • Overview of Methods for Identification of Collagen Protein

  Collagen is a widely present structural protein in animal tissues, especially in the skin, bones, tendons, ligaments, and many other connective tissues. Due to its crucial role in maintaining tissue structure and function, the identification of collagen is highly important for biomedical research and clinical diagnosis.