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Related Concept Videos

Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...

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Related Experiment Video

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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Transmembrane helix dimerization: beyond the search for sequence motifs.

Edwin Li1, William C Wimley, Kalina Hristova

  • 1Department of Biology, Saint Joseph's University, Philadelphia, PA 19131, USA.

Biochimica Et Biophysica Acta
|September 14, 2011
PubMed
Summary

Transmembrane helix dimerization is key to membrane protein folding. While sequence motifs were thought to explain these interactions, new evidence reveals a more complex picture beyond simple sequence patterns.

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Last Updated: May 29, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Published on: May 26, 2011

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Transmembrane (TM) helix dimerization is crucial for understanding membrane protein (MP) folding.
  • The prevailing model for TM helix interactions relies on sequence motifs, which are specific amino acid sequences driving lateral associations.
  • However, the characterization of diverse interacting helices challenges the sufficiency of the sequence motif paradigm.

Purpose of the Study:

  • To review the evolution of understanding TM helix dimerization.
  • To highlight the limitations of the sequence motif model in explaining MP folding.
  • To present a more complex view of TM helix interactions.

Main Methods:

  • Literature review of experimental and theoretical studies on TM helix dimerization.
  • Analysis of the historical development of models for TM helix interactions.
  • Synthesis of current understanding regarding the complexity of TM helix associations.

Main Results:

  • The sequence motif paradigm, while influential, is insufficient to fully explain TM helix dimerization.
  • Experimental data increasingly points to complexities beyond simple sequence-based interactions.
  • A broader perspective is needed to understand the intricate forces governing TM helix associations.

Conclusions:

  • The understanding of TM helix dimerization has moved beyond the simplistic sequence motif model.
  • Predicting and explaining TM helix interactions requires consideration of more complex factors.
  • Further research is needed to fully elucidate the multifaceted nature of membrane protein folding.