Chemical labeling strategies for recognition and determination of protein and peptide

2011 ◽  
Vol 41 (4) ◽  
pp. 663-677 ◽  
Author(s):  
XiaoWen YAN ◽  
LiMin YANG ◽  
QiuQuan WANG ◽  
Ming XU
Keyword(s):  
Chemical Labeling ◽  
Labeling Strategies

Evaluation of chemical labeling strategies for monitoring HCV RNA using vibrational microscopy

2007 ◽  
Vol 5 (15) ◽  
pp. 2380 ◽  
Author(s):  
Matthew Noestheden ◽  
Qingyan Hu ◽  
Angela M. Tonary ◽  
Li-Lin Tay ◽  
John Paul Pezacki
Keyword(s):  
Hcv Rna ◽  
Chemical Labeling ◽  
Labeling Strategies

Chemical labeling strategies for cell biology

2006 ◽  
Vol 3 (8) ◽  
pp. 591-596 ◽  
Author(s):  
Kevin M Marks ◽  
Garry P Nolan
Keyword(s):  
Cell Biology ◽  
Chemical Labeling ◽  
Labeling Strategies

scholarly journals Combined Metabolic and Chemical (CoMetChem) Labeling Using Stable Isotopes – a Strategy to Reveal Site-Specific Histone Acetylation and Deacetylation Rates by LC-MS

2021 ◽  
Author(s):  
Alienke van Pijkeren ◽  
Jörn Dietze ◽  
Alejandro Sánchez Brotons ◽  
Tim Lijster ◽  
Andrei Barcaru ◽  
...  
Keyword(s):  
Histone Acetylation ◽  
Protein Modification ◽  
High Resolution Mass Spectrometry ◽  
Reaction Rates ◽  
Lysine Acetylation ◽  
Chemical Labeling ◽  
Comprehensive Description ◽  
Site Specific ◽  
New Approach

Histone acetylation is an important, reversible post-translational protein modification and a hallmark of epigenetic regulation. However, little is known about the dynamics of this process, due to the lack of analytical methods that can capture site-specific acetylation and deacetylation reactions. We present a new approach that combines metabolic and chemical labeling (CoMetChem) using uniformly 13C-labeled glucose and stable isotope labeled acetic anhydride. Thereby, chemically equivalent, fully acetylated histone species are generated enabling accurate relative quantification of site-specific lysine acetylation in tryptic peptides using high-resolution mass spectrometry. We show that CoMetChem enables site-specific quantification of the incorporation or loss of lysine acetylation over time, allowing the determination of reaction rates for acetylation and deacetylation. Thus, the CoMetChem methodology provides a comprehensive description of site-specific acetylation dynamics. <br>

scholarly journals Combined Metabolic and Chemical (CoMetChem) Labeling Using Stable Isotopes – a Strategy to Reveal Site-Specific Histone Acetylation and Deacetylation Rates by LC-MS

2021 ◽  
Author(s):  
Alienke van Pijkeren ◽  
Jörn Dietze ◽  
Alejandro Sánchez Brotons ◽  
Tim Lijster ◽  
Andrei Barcaru ◽  
...  
Keyword(s):  
Histone Acetylation ◽  
Protein Modification ◽  
High Resolution Mass Spectrometry ◽  
Reaction Rates ◽  
Lysine Acetylation ◽  
Chemical Labeling ◽  
Comprehensive Description ◽  
Site Specific ◽  
New Approach

Histone acetylation is an important, reversible post-translational protein modification and a hallmark of epigenetic regulation. However, little is known about the dynamics of this process, due to the lack of analytical methods that can capture site-specific acetylation and deacetylation reactions. We present a new approach that combines metabolic and chemical labeling (CoMetChem) using uniformly 13C-labeled glucose and stable isotope labeled acetic anhydride. Thereby, chemically equivalent, fully acetylated histone species are generated enabling accurate relative quantification of site-specific lysine acetylation in tryptic peptides using high-resolution mass spectrometry. We show that CoMetChem enables site-specific quantification of the incorporation or loss of lysine acetylation over time, allowing the determination of reaction rates for acetylation and deacetylation. Thus, the CoMetChem methodology provides a comprehensive description of site-specific acetylation dynamics. <br>

Sign in / Sign up

Export Citation Format

Share Document