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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...
Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell types have...
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...
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

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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.
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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 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.
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Updated: May 13, 2026

Creating and Applying a Reference to Facilitate the Discussion and Classification of Proteins in a Diverse Group
07:49

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Published on: August 16, 2017

Alignment of helical membrane protein sequences using AlignMe.

Marcus Stamm1, René Staritzbichler, Kamil Khafizov

  • 1Computational Structural Biology Group, Max Planck Institute of Biophysics, Frankfurt am Main, Germany. k46581a@nucc.cc.nagoya-u.ac.jp

Plos One
|March 8, 2013
PubMed
Summary
This summary is machine-generated.

We developed AlignMePS, a new method for aligning integral membrane protein sequences that combines evolutionary and secondary structure information for high accuracy. AlignMePST, which also includes transmembrane segment matching, is best for distantly related proteins.

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Last Updated: May 13, 2026

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Area of Science:

  • Bioinformatics
  • Computational Biology
  • Structural Biology

Background:

  • Integral membrane proteins possess unique evolutionary and structural characteristics not fully addressed by standard sequence alignment methods.
  • Existing methods often incorporate membrane information via specialized substitution matrices or differential gap penalties for transmembrane regions.

Purpose of the Study:

  • To evaluate if incorporating predicted transmembrane segments into standard dynamic programming algorithms can enhance the accuracy of pairwise integral membrane protein sequence alignments.
  • To optimize alignment strategies for integral membrane proteins using a dedicated program, AlignMe, and a curated dataset of homologous membrane protein structures (HOMEP2).

Main Methods:

  • Development and testing of various alignment strategies within the AlignMe program.
  • Optimization of gap penalties using the HOMEP2 dataset of homologous membrane protein structures.
  • Evaluation of optimized methods on the BAliBASE collection of membrane protein sequence alignments.

Main Results:

  • The AlignMePS approach, integrating secondary structure matching (S) with evolutionary information (position-specific substitution matrix, P), yielded highly accurate pairwise alignments across diverse sequence similarities.
  • The AlignMePST approach, adding transmembrane prediction matching (T) to AlignMePS, showed reduced accuracy for closely related proteins but may benefit alignments of very distantly related proteins.

Conclusions:

  • AlignMePS offers a significant improvement in accuracy for integral membrane protein sequence alignment, particularly when combining evolutionary and secondary structure information.
  • AlignMePST provides a potential advantage for aligning extremely divergent membrane protein sequences where traditional sequence information is limited.
  • The AlignMe software, associated datasets, and an online server are publicly available for research use.