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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 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...
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...
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...
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...
Protein Organization01:13

Protein Organization

Overview

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Related Experiment Video

Updated: Jun 4, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

The MEMPACK alpha-helical transmembrane protein structure prediction server.

Timothy Nugent1, Sean Ward, David T Jones

  • 1Department of Computer Science, University College London, London, UK. t.nugent@cs.ucl.ac.uk

Bioinformatics (Oxford, England)
|February 26, 2011
PubMed
Summary
This summary is machine-generated.

MEMPACK is a new tool that predicts the structure of alpha-helical transmembrane proteins using machine learning. It provides detailed predictions of topology, lipid exposure, and helix interactions, aiding in protein structure determination.

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Last Updated: Jun 4, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
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Published on: July 8, 2025

Area of Science:

  • Structural bioinformatics
  • Computational biology
  • Biophysics

Background:

  • Alpha-helical transmembrane proteins are crucial but experimentally challenging to study.
  • Accurate structure determination is vital for understanding protein function.
  • Sequence-based prediction tools are essential for this protein class.

Purpose of the Study:

  • To introduce MEMPACK, a novel prediction server for transmembrane protein structures.
  • To provide users with detailed predictions of protein topology and interactions.
  • To leverage machine learning for enhanced structure prediction.

Main Methods:

  • Development of novel machine learning algorithms.
  • Implementation of a user-friendly web server (MEMPACK).
  • Prediction of transmembrane topology, lipid exposure, residue contacts, and helix interactions.

Main Results:

  • MEMPACK successfully predicts various structural features of alpha-helical transmembrane proteins.
  • The server offers predictions in both text and graphical formats.
  • It provides insights into helix-helix interactions and packing arrangements.

Conclusions:

  • MEMPACK offers a valuable resource for researchers studying transmembrane proteins.
  • The tool enhances the capabilities of sequence-based structure prediction.
  • Accessible via the PSIPRED portal, MEMPACK facilitates structural analysis.