相关实验视频
Updated: Jul 18, 2025

13:09
Mass Spectrometric Analysis of Glycosphingolipid Antigens
Published on: April 16, 2013
16.6K
通过MS和机器学习――使用酸链接的概念验证,自动推断甘氨酸链接
Xinyi Ni1, Nathan B Murray2, Stephanie Archer-Hartmann2
1Computer Science, Brandeis University, Waltham, Massachusetts 02453, United States.
Journal of the American Society for Mass Spectrometry
|August 24, 2023
概括
这项研究引入了一种机器学习框架,以优化质谱法 (MS) 协议,用于分析寡糖类糖链接. 该方法使用低能量的MS碎片化准确识别酸链接,减少样本要求和实验时间.
科学领域:
- 碳水化合物化学 碳水化合物化学
- 分析化学 分析化学
- 生物化学 生物化学
背景情况:
- 寡糖类中的甘氨酸链接对于它们的化学性质和生物功能至关重要.
- 质谱法 (MS) 是推断这些联系的关键技术,但通常需要大量的样本数量,缺乏标准化的协议.
- 需要严格的研究来建立最佳的MS协议,以准确地表征糖酸链接.
研究的目的:
- 开发基于机器学习的框架,以建立适当的MS协议和数据分析方法,以阐明寡糖的联系.
- 为了证明该框架在标准和N-glycans中表征酸链接 (α2'-3'和α2'-6') 的有效性.
- 为了实现高质量的实验数据生成和分析,以确定甘氨酸链接.
主要方法:
- 实施机器学习框架以优化MS协议和数据分析.
- 该框架应用于酸乳糖标准和NIST含酸的N-甘氨酸.
- 使用各种MS碎片化水平 (MS2-MS5) 进行链接分析.
主要成果:
- 确定最佳的MS协议配置,以获得高质量的数据.
- 在使用MS2-MS5光谱对α2′-3′与α2′-6′酸链接进行分类时,获得了近100%的准确性.
- 证明了使用MS5光谱预测含有8.6%RMSE的混合物中的链接比率的能力.
结论:
- 开发的机器学习框架使得精确和高效的甘氨酸链接分析成为可能,即使样本数量有限.
- 低能量的MS碎片化 (MS2,MS3) 足以准确地确定链接,减少样本需求和实验时间.
- 该框架显示,它有望在分析甘氨酸和合成材料中的各种甘氨酸链接方面得到更广泛的应用.
相关概念视频
Mass Spectrometry: Complex Analysis
822
Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
822
Peptide Identification Using Tandem Mass Spectrometry
6.5K
Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
6.5K
Oligosaccharide Assembly
2.9K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
2.9K
Protein Glycosylation
7.0K
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Glycosylation occurs in...
7.0K

