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...
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...
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
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...

You might also read

Related Articles

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

Sort by
Same author

Machine-Learned Leftmost Hessian Eigenvectors for Robust Transition State Finding.

Journal of chemical theory and computation·2026
Same author

Energetics of Noncovalent Interactions of Protein-Ligand Complexes for Drug Discovery.

Journal of chemical information and modeling·2026
Same author

Sensing the acidity of hydrogen bond networks.

Physical chemistry chemical physics : PCCP·2026
Same author

SmileyLlama: modifying large language models for directed chemical space exploration.

Nature computational science·2026
Same author

Conformational Ensembles of the Disordered 4E-BP2:eIF4E Complex Restrained by smFRET Experiments.

bioRxiv : the preprint server for biology·2026
Same author

LinkLlama: Enabling Large Language Model for Chemically Reasonable Linker Design.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Jun 10, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Driving forces for transmembrane alpha-helix oligomerization.

Alex J Sodt1, Teresa Head-Gordon

  • 1Department of Bioengineering, University of California, Berkeley, California, USA. alexsodt@berkeley.edu

Biophysical Journal
|July 27, 2010
PubMed
Summary

We developed a new statistical method to predict amino acid interactions in transmembrane alpha-helical bundles. Polarity, not size, primarily drives these helix-helix interface interactions, aiding protein structure prediction.

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

Characterization of Multi-subunit Protein Complexes of Human MxA Using Non-denaturing Polyacrylamide Gel-electrophoresis
08:55

Characterization of Multi-subunit Protein Complexes of Human MxA Using Non-denaturing Polyacrylamide Gel-electrophoresis

Published on: October 28, 2016

Related Experiment Videos

Last Updated: Jun 10, 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

Characterization of Multi-subunit Protein Complexes of Human MxA Using Non-denaturing Polyacrylamide Gel-electrophoresis
08:55

Characterization of Multi-subunit Protein Complexes of Human MxA Using Non-denaturing Polyacrylamide Gel-electrophoresis

Published on: October 28, 2016

Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Biology

Background:

  • Transmembrane (TM) alpha-helical bundles are crucial protein structures.
  • Understanding helix-helix interfaces is key to predicting protein function and structure.

Purpose of the Study:

  • To develop a novel statistical contact potential for analyzing amino acid interactions in TM alpha-helical bundles.
  • To investigate the role of amino acid properties, particularly polarity and size, in stabilizing helix-helix interfaces.

Main Methods:

  • Developed a statistical contact potential based on solved TM alpha-helical bundle structures.
  • Reduced the contact energy matrix to a four-flavor amino acid alphabet for enhanced statistical significance.
  • Utilized two-body contact energies and sequence correlations for structure prediction analysis.

Main Results:

  • Identified polarity as a more dominant factor than size in amino acid grouping for helix interfaces.
  • Observed that charged/polar groups favor the same face, while polar/apolar pairs favor opposite faces.
  • Demonstrated that two-body contact energies can predict native structures from decoys for many TM proteins.

Conclusions:

  • The novel statistical contact potential effectively models helix-helix interface stabilization.
  • Amino acid polarity plays a significant role in TM protein structure, even for rare residues.
  • Higher-order sequence correlations are necessary for highly accurate TM protein structure predictions.