Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Energy to Drive Translocation01:37

Energy to Drive Translocation

Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
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...
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...

You might also read

Related Articles

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

Sort by
Same author

Pore Geometry-Driven Capture of Trace Aromatic Volatile Organic Compounds in Al-Based MOFs.

ACS nano·2026
Same author

Tunable Microporous Bimetallic Carboxylate-Pyrazolate Metal-Organic Frameworks for CO<sub>2</sub> Capture.

Journal of the American Chemical Society·2026
Same author

The data-only illusion in materials discovery.

Nature materials·2026
Same author

Machine learning potential for modelling dynamic hydrogen bond networks in MOF MIL-120.

Chemical science·2026
Same author

Peer Review and AI: Your (Human) Opinion Is What Matters.

ACS nano·2026
Same author

Lead, Locked Away: Porous Zr-Phytate Coordination Polymers for Rapid and Selective Removal of Pb<sup>2+</sup> from Water.

Journal of the American Chemical Society·2025
Same journal

Quantifying the Peripheral Surface Information Entropy from Conformational Ensembles of Globular Protein-Peptide Complexes.

Biophysical journal·2026
Same journal

Anisotropic unbinding and location-dependent hovering of a kinesin motor head over microtubule.

Biophysical journal·2026
Same journal

Kinesin-5/Cut7 C-terminal tail phosphorylation influence on motor regulation through multi-scale molecular modeling.

Biophysical journal·2026
Same journal

Dynamic conformations of fluorophores on self-labeling protein tags.

Biophysical journal·2026
Same journal

Different actions of RyR2 open and closed channel block explained by a multiscale Ca<sup>2+</sup> release model.

Biophysical journal·2026
Same journal

Membrane Environment Sets the Functional pK<sub>a</sub> of Ionizable Lipids.

Biophysical journal·2026
See all related articles

Related Experiment Video

Updated: May 18, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Robust driving forces for transmembrane helix packing.

Ayelet Benjamini1, Berend Smit

  • 1Department of Chemistry, University of California, Berkeley, California, USA.

Biophysical Journal
|September 22, 2012
PubMed
Summary
This summary is machine-generated.

The lipid environment, not just residue patterns, dictates transmembrane helix packing. Hydrophobic mismatch between proteins and lipids is the primary driver of helix cross-angle distribution in membranes.

More Related Videos

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

High-Speed Magnetic Tweezers for Nanomechanical Measurements on Force-Sensitive Elements
08:50

High-Speed Magnetic Tweezers for Nanomechanical Measurements on Force-Sensitive Elements

Published on: May 12, 2023

Related Experiment Videos

Last Updated: May 18, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

High-Speed Magnetic Tweezers for Nanomechanical Measurements on Force-Sensitive Elements
08:50

High-Speed Magnetic Tweezers for Nanomechanical Measurements on Force-Sensitive Elements

Published on: May 12, 2023

Area of Science:

  • Biophysics
  • Structural Biology
  • Membrane Protein Dynamics

Background:

  • Transmembrane helix packing is traditionally explained by residue interactions at contact surfaces.
  • The influence of the lipid bilayer environment on helix structure has been considered minor.

Purpose of the Study:

  • To investigate the role of the lipid environment in determining transmembrane helix packing.
  • To analyze the factors controlling the cross-angle distribution of packed helices.

Main Methods:

  • Analysis of structural data from a membrane protein database.
  • Molecular simulations using a coarse-grained model without specific residue interactions.

Main Results:

  • The cross-angle distribution of helix pairs in the database matches that of non-interacting helices in a membrane.
  • Helix tilt angles, influenced by hydrophobic mismatch, largely determine the cross angle.
  • Simulations confirm the database's cross-angle distribution, independent of specific residue interactions.

Conclusions:

  • Hydrophobic mismatch is the dominant factor in transmembrane helix packing.
  • The lipid environment significantly influences helix structure and packing.
  • Short-range forces play a secondary role in fine-tuning the final helix configuration.