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Related Concept Videos

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...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

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Related Experiment Video

Updated: Jun 17, 2026

Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry
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TIM-Finder: a new method for identifying TIM-barrel proteins.

Jing-Na Si1, Ren-Xiang Yan, Chuan Wang

  • 1State Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing 100193, China. sijingna@gmail.com

BMC Structural Biology
|December 17, 2009
PubMed
Summary
This summary is machine-generated.

A new computational tool, TIM-Finder, enhances the identification of triosephosphate isomerase (TIM)-barrel proteins. This method improves proteome-wide analysis and accelerates protein discovery.

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Area of Science:

  • Bioinformatics
  • Computational Biology
  • Structural Biology

Background:

  • The triosephosphate isomerase (TIM)-barrel fold is prevalent across organisms, with diverse protein functions.
  • Sensitive detection of TIM-barrel proteins is crucial for exploring their sequence-structure landscape.

Purpose of the Study:

  • To develop an advanced computational tool for sensitive and accurate identification of TIM-barrel proteins.
  • To improve upon existing methods for TIM-barrel protein detection in proteomic datasets.

Main Methods:

  • Integration of three descriptors: sequence-alignment (PSI-BLAST e-values/bit scores), secondary structure element alignment (SSEA), and PROSITE functional motifs.
  • Application of Support Vector Machine (SVM) for descriptor combination and model training.
  • Validation using the complete proteome of Bacillus subtilis.

Main Results:

  • The developed method, TIM-Finder, demonstrates superior performance in TIM-barrel protein identification.
  • TIM-Finder identified 194 TIM-barrel proteins in Bacillus subtilis at a 99% confidence level.
  • Outperformed standard PSI-BLAST searches and existing fold recognition methods.

Conclusions:

  • TIM-Finder is a competitive and effective tool for proteome-wide TIM-barrel protein identification.
  • The TIM-Finder web server is publicly accessible for research use.