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Related Concept Videos

Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Conservation of Protein Domains Over Different Proteins02:26

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Evolutionary Relationships through Genome Comparisons02:54

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Genome comparison is one of the excellent ways to interpret the evolutionary relationships between organisms. The basic principle of genome comparison is that if two species share a common feature, it is likely encoded by the DNA sequence conserved between both species. The advent of genome sequencing technologies in the late 20th century enabled scientists to understand the concept of conservation of domains between species and helped them to deduce evolutionary relationships across diverse...
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Related Experiment Video

Updated: Oct 15, 2025

A Virtual Machine Platform for Non-Computer Professionals for Using Deep Learning to Classify Biological Sequences of Metagenomic Data
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Predicting subcellular location of protein with evolution information and sequence-based deep learning.

Zhijun Liao1,2, Gaofeng Pan2, Chao Sun2

  • 1Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Fujian Medical University, 1 Xuefu North Road, University Town, Fuzhou, 350122, FJ, China.

BMC Bioinformatics
|October 23, 2021
PubMed
Summary
This summary is machine-generated.

This study introduces a novel deep learning method for predicting protein subcellular localization, outperforming existing techniques by incorporating evolutionary information for improved accuracy in biological research.

Keywords:
Deep learningEvolution informationMultiple label classificationProtein sequenceSubcellular prediction

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Area of Science:

  • Computational Biology
  • Bioinformatics
  • Molecular Biology

Background:

  • Protein subcellular localization is crucial for understanding biological functions.
  • Traditional prediction methods are often laborious and time-consuming.
  • Existing machine learning methods frequently overlook protein evolutionary information.

Purpose of the Study:

  • To develop an accurate deep learning-based method for protein subcellular localization prediction.
  • To integrate evolutionary information into the prediction model.
  • To enhance the precision of subcellular location predictions.

Main Methods:

  • Utilized a deep learning architecture combining bidirectional long short-term memory (LSTM) and convolutional neural networks (CNN).
  • Incorporated amino acid composition, protein sequences, and evolution matrices (Position-Specific Scoring Matrix - PSSM).
  • Trained and validated the model on two benchmark datasets.

Main Results:

  • Achieved an average precision of 0.7901, ranking loss of 0.0758, and coverage of 1.2848 on benchmark datasets.
  • Demonstrated superior performance compared to five existing prediction methods.
  • The model effectively extracts features from protein sequences and evolutionary data.

Conclusions:

  • The proposed deep learning method offers an accurate and acceptable alternative for protein subcellular localization prediction.
  • Integrating evolutionary information significantly improves prediction accuracy.
  • The method's performance highlights the importance of sequence and evolutionary data in bioinformatics.