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Related Concept Videos

Covalently Linked Protein Regulators02:04

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 Regulators02:04

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.
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Protein Modifications in the RER01:26

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.
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...

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Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis
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Published on: October 18, 2024

Protein modifications giving rise to homo-oligomers.

Georg E Schulz1

  • 1Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Freiburg im Breisgau, Germany.

Progress in Molecular Biology and Translational Science
|October 18, 2011
PubMed
Summary

Protein engineering advances enable designing protein self-assembly into homo-oligomers. Achieving specific, asymmetric protein assemblies (multiplicity one) is challenging but crucial for novel nanomaterials.

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Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis
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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

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Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
12:43

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

Published on: July 27, 2016

Area of Science:

  • Protein engineering
  • Biomolecular design
  • Nanotechnology

Background:

  • Atomic-level protein structures are known.
  • Large-scale protein production is feasible.
  • Protein self-assembly offers engineering potential.

Purpose of the Study:

  • To explore the design of protein molecules associating into homo-oligomers.
  • To present worked examples of designed protein associations.
  • To investigate rules governing protein surface properties for assembly.

Main Methods:

  • Analysis of protein structures and symmetries.
  • Application of the multiplicity concept in protein design.
  • Identification and discussion of mutations for surface property modification.

Main Results:

  • Worked examples of flexible/rigid and fixed/switchable protein associations are presented.
  • The multiplicity concept and symmetry are key to protein assembly design.
  • Achieving asymmetric assemblies (multiplicity one) is difficult.

Conclusions:

  • Protein engineering can guide self-assembly for nanomaterial development.
  • Understanding symmetry and multiplicity is vital for controlling protein associations.
  • New rules for surface properties are proposed to facilitate desired protein assemblies.