Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Covalently Linked Protein Regulators

Covalently 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.

Protein Modifications in the RER

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Isosteric Engineering of Enzymes: Overcoming Activity-Stability Trade-Offs by Site-Selective CH → N Substitutions.

Angewandte Chemie (International ed. in English)·2026

Same author

Harnessing the Reactivity of Sulfinate Salts With Cystine: An Umpolung Approach to Residue-Specific Peptide Modification.

Angewandte Chemie (International ed. in English)·2026

Same author

Advances in electrochemical peptide synthesis and modification.

Nature reviews. Chemistry·2026

Same author

PYEAST - A Computational Toolkit for Saccharomyces cerevisiae Genetic Engineering.

NPJ systems biology and applications·2026

Same author

Advances in polarised luminescence approaches to understanding interactions between biomolecules.

Biochemical Society transactions·2026

Same author

Biosynthetic Lanthanide-Luminescent Mini-Proteins Using Genetic Code Expansion.

Journal of the American Chemical Society·2026

Search research articles

Related Experiment Video

Updated: May 13, 2026

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

Published on: January 27, 2016

Iso-pseudoprolines as versatile tools for late-stage peptide backbone modifications.

Karen D Milewska^1,2, Brett D Schwartz^1,2, Jemimah R Canning^1,2

¹Research School of Chemistry, Australian National University Canberra ACT 2601 Australia lara.malins@anu.edu.au.

Chemical Science

|February 20, 2026

Summary

This study introduces novel iso-pseudoprolines, thiazolidine-2-carboxylic acid (2-Thz) and selenazolidine-2-carboxylic acid (2-Sez), for peptide design. These residues enable late-stage peptide backbone modification via reductive ring opening, creating diverse peptoid derivatives.

More Related Videos

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

An Inexpensive Adaptation of a Commercial Microwave Reactor for Solid Phase Peptide Synthesis

An Inexpensive Adaptation of a Commercial Microwave Reactor for Solid Phase Peptide Synthesis

Published on: November 22, 2024

Related Experiment Videos

Last Updated: May 13, 2026

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

Published on: January 27, 2016

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

An Inexpensive Adaptation of a Commercial Microwave Reactor for Solid Phase Peptide Synthesis

An Inexpensive Adaptation of a Commercial Microwave Reactor for Solid Phase Peptide Synthesis

Published on: November 22, 2024

Area of Science:

Chemical Biology
Medicinal Chemistry
Synthetic Chemistry

Background:

Proline and its mimetics are crucial for designing bioactive peptides.
Pseudoprolines from serine, threonine, and cysteine are well-studied.
Regioisomeric iso-pseudoprolines, with heteroatoms at the beta-carbon, are less explored.

Purpose of the Study:

To investigate the incorporation and utility of thiazolidine-2-carboxylic acid (2-Thz) and selenazolidine-2-carboxylic acid (2-Sez) in peptides and proteins.
To establish these iso-pseudoprolines as versatile building blocks for peptide modification.

Main Methods:

Incorporation of 2-Thz and 2-Sez into peptides and proteins using synthetic and biosynthetic methods.
Reductive ring opening of the iso-pseudoproline residues.
Late-stage functionalization of the resulting thiol/selenol handles with electrophiles.

Main Results:

Demonstrated successful incorporation of 2-Thz and 2-Sez into peptide backbones.
Established reductive ring opening as a method for late-stage peptide modification.
Generated diverse peptoid derivatives by trapping nucleophilic handles with various electrophiles.

Conclusions:

Thiazolidine-2-carboxylic acid and selenazolidine-2-carboxylic acid are valuable iso-pseudoproline building blocks.
These residues provide a novel platform for late-stage diversification of peptides and proteins.
The developed methodology allows for the synthesis of unique peptoid structures.