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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.

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.

Bacterial Protein Maturation

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

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.

Mutations

Mutations

Mutations

Mutations

Mutations are changes in the sequence of DNA. These changes can occur spontaneously or they can be induced by exposure to environmental factors. Mutations can be characterized in a number of different ways: whether and how they alter the amino acid sequence of the protein, whether they occur over a small or large area of DNA, and whether they occur in somatic cells or germline cells.
Chromosomal Alterations Are Large-Scale Mutations
While point mutations are changes in a single nucleotide in...

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Related Experiment Video

Updated: May 19, 2026

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations

Published on: April 26, 2024

Post-translational modifications induce significant yet not extreme changes to protein structure.

Fuxiao Xin¹, Predrag Radivojac

¹School of Informatics and Computing, Indiana University, Bloomington, IN, USA.

Bioinformatics (Oxford, England)

|September 6, 2012

Summary

Post-translational modifications (PTMs) cause protein structural changes, but large rearrangements are rare. Phosphorylation, a common PTM, stabilizes protein structure by reducing overall flexibility.

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Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications

Published on: May 18, 2017

Related Experiment Videos

Last Updated: May 19, 2026

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations

Published on: April 26, 2024

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications

Published on: May 18, 2017

Area of Science:

Biochemistry
Structural Biology
Bioinformatics

Background:

Post-translational modifications (PTMs) are known to induce protein structural changes.
Previous studies often highlighted large conformational changes, potentially overlooking subtler effects.
The growing Protein Data Bank (PDB) enables systematic analysis of PTMs' roles as conformational switches.

Purpose of the Study:

To systematically characterize the extent and nature of structural changes induced by PTMs.
To determine the frequency of substantial conformational changes upon PTM.
To investigate whether PTMs induce localized or global structural impacts and if different PTMs have distinct signatures.

Main Methods:

Utilized redundancy in the PDB to compare structures of identical protein sequences in unmodified and modified forms.
Employed root-mean-square deviation (RMSD) to quantify conformational heterogeneity.
Focused analysis on glycosylation and phosphorylation, also examining acetylation and methylation.

Main Results:

PTMs induce both local and global conformational changes in proteins.
Large global changes (>2 Å) are infrequent: 7% for glycosylation, 13% for phosphorylation.
Phosphorylation was found to stabilize protein structure, reducing global conformational heterogeneity by 25%.

Conclusions:

PTMs play a subtle yet common role in regulating protein function through allostery.
The majority of PTM-induced structural changes are not dramatic.
Understanding these subtle shifts is crucial for deciphering regulatory and signaling pathways.