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Related Concept Videos

Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

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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...
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Structure of Porins01:21

Structure of Porins

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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
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Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

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Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
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Assembly of the Lipid Bilayer in the ER01:28

Assembly of the Lipid Bilayer in the ER

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Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
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Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

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For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Updated: Mar 12, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
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From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

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Counting strands in outer membrane β-barrels.

Samuel Lim1, Tejaswi Nimmagadda1, Alaa Khamis2

  • 1Computational Biology Program, The University of Kansas, Lawrence, Kansas.

Biophysical Journal
|March 11, 2026
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Summary
This summary is machine-generated.

A new algorithm accurately counts beta-barrel protein strands in bacterial outer membranes. This tool enhances understanding of protein structure and function, aiding future research in prediction and design.

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A Nanobar-Supported Lipid Bilayer System for the Study of Membrane Curvature Sensing Proteins in vitro
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Area of Science:

  • Structural biology
  • Computational biology
  • Biochemistry

Background:

  • Beta-barrel proteins are essential in bacterial outer membranes, mediating transport and structural integrity.
  • Accurate determination of beta-barrel strand count is crucial for understanding protein function but challenging due to structural complexities.

Purpose of the Study:

  • To refine the PolarBearal tool for accurate, large-scale identification of beta-barrel strand numbers.
  • To create a comprehensive dataset of outer membrane beta-barrel structures with labeled strand counts.

Main Methods:

  • Developed an updated algorithm integrating inter-residue vector angles, hydrogen-bonding distances, and strand connectivity.
  • Applied the algorithm to analyze 571,760 predicted outer membrane beta-barrel structures from the AlphaFold2 database.

Main Results:

  • Achieved 97% accuracy in assigning strand numbers for beta-barrel structures.
  • Generated a large dataset enabling assessment of strand count homogeneity across different outer membrane protein types.

Conclusions:

  • The refined PolarBearal algorithm provides accurate beta-barrel strand labeling for large datasets.
  • The resulting data offers insights into beta-barrel distribution and evolutionary patterns, supporting protein structure prediction and design.