Related Experiment Video
Updated: Dec 29, 2025

06:31
"Cell Surface Capture" Workflow for Label-Free Quantification of the Cell Surface Proteome
Published on: March 24, 2023
2.9K
FTIP: an accurate and efficient method for global protein surface comparison
Yuan Zhang1, Xing Sui1, Scott Stagg2
1Department of Statistics.
Bioinformatics (Oxford, England)
|February 6, 2020
Summary
A new method, Farthest Point Sampling (FPS)-enhanced Triangulation-based Iterative-Closest-Point (ICP) (FTIP), improves global protein surface comparison (GPSC). FTIP shows promise for protein identification in cryo-electron tomography (CET) experiments.
Area of Science:
- Structural biology
- Computational biology
- Biophysics
Background:
- Global protein surface comparison (GPSC) has lacked practical applications, limiting its research scope.
- Advances in cryo-electron tomography (CET) highlight the need for effective protein identification methods based on surface shape.
Purpose of the Study:
- To develop and evaluate a novel method for GPSC that utilizes only surface shape information.
- To assess the method's performance in protein classification and its potential application in CET.
Main Methods:
- Developed the Farthest Point Sampling (FPS)-enhanced Triangulation-based Iterative-Closest-Point (ICP) (FTIP) algorithm for GPSC.
- Extracted feature points using FPS and employed a triangulation-based ICP algorithm for alignment.
- Applied nearest-neighbor classification on a benchmark dataset of 2329 proteins.
Main Results:
- FTIP outperformed the state-of-the-art 3D Zernike descriptor method for GPSC.
- The method demonstrated successful protein classification using only surface shape.
- FTIP showed potential for protein identification in real and simulated CET data.
Conclusions:
- FTIP offers a robust and efficient approach to global protein surface comparison.
- The method has significant potential for advancing protein identification in cryo-electron tomography.
- The developed software is publicly available for further research and application.
Related Concept Videos
Protein-protein Interfaces
14.4K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.4K
Conserved Binding Sites
5.0K
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...
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...
5.0K

