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Covalently Linked Protein Regulators

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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.
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Related Experiment Video

Updated: Mar 14, 2026

Designing Silk-silk Protein Alloy Materials for Biomedical Applications

Designing Silk-silk Protein Alloy Materials for Biomedical Applications

Published on: August 13, 2014

Post-translational modifications of silk proteins.

Kota Nomura¹, Keiji Numata^1,2

¹Department of Material Chemistry, Graduate School of Engineering, Kyoto University Kyoto 615-8510 Japan keiji.numata@riken.jp.

RSC Chemical Biology

|March 13, 2026

Summary

Post-translational modifications (PTMs) add chemical diversity to silk proteins, influencing their assembly and properties. Understanding these modifications is key to designing advanced protein-based materials.

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Area of Science:

Biomaterials Science
Chemical Biology
Protein Chemistry

Background:

Silk proteins possess inherent chemical diversity due to post-translational modifications (PTMs).
PTMs critically influence silk's higher-order assembly, hydration, and structural integrity.
Key PTMs include hydroxylation, glycosylation, phosphorylation, and covalent crosslinking.

Purpose of the Study:

To review the principal PTMs in silk proteins and their functional impact.
To highlight recent advances in PTM discovery and engineering.
To establish a foundation for designing novel silk-based materials.

Main Methods:

Literature review of PTMs in silk proteins.
Discussion of proteomics advancements for PTM identification.
Exploration of synthetic biology and bioorthogonal chemistry for PTM manipulation.

Main Results:

PTMs significantly contribute to silk protein structural stability and mechanical properties.
Low-abundance PTMs are increasingly being identified through advanced proteomics.
Engineered PTMs can tune the physicochemical properties of silk.

Conclusions:

Harnessing PTMs is crucial for understanding and controlling silk protein behavior.
Predictive design of next-generation silk-based materials relies on PTM knowledge.
This work bridges chemical biology and materials science for advanced biomaterial development.