Related Experiment Video
Updated: May 17, 2026
12:11
Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
Published on: February 27, 2020
Modeling methods for studying post-translational and transcriptional modifying enzymes
Maite Roca1, Juan Aranda, Vicent Moliner
1Departamento de Química Física, Universitat de València, 46100 Burjassot, Spain.
Current Opinion in Chemical Biology
|November 7, 2012
Summary
Computational methods offer insights into complex biological catalysis, particularly for post-transcriptional and post-translational modifications involving biomacromolecules. This review examines modeling strategies for these processes.
Area of Science:
- Biochemistry
- Computational Chemistry
- Molecular Biology
Background:
- Biological catalysis involves intricate electronic and structural changes in substrates and catalysts.
- Post-transcriptional and post-translational modifications add complexity due to biomacromolecular interactions.
Purpose of the Study:
- To review computational modeling efforts for catalysis in post-transcriptional and post-translational modifications.
- To analyze the advantages and limitations of various computational strategies.
Main Methods:
- Review of recent computational studies on biological catalysis.
- Analysis of modeling techniques for biomacromolecular interactions in catalysis.
Main Results:
- Computational methods provide detailed molecular insights into catalytic events.
- Understanding reaction mechanisms in biological systems is enhanced.
Conclusions:
- Computational strategies are crucial for understanding complex biological catalysis.
- The applicability and challenges of different modeling approaches are highlighted.
Related Concept Videos
02:04Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
02:54Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
02:32Histone Modification
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...