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Updated: Jan 24, 2026

A Graphical User Interface for Software-assisted Tracking of Protein Concentration in Dynamic Cellular Protrusions

A Graphical User Interface for Software-assisted Tracking of Protein Concentration in Dynamic Cellular Protrusions

Published on: July 11, 2017

AlphaFold時代のタンパク質相互作用部位予測：ダイナミクスと無秩序が依然として課題である理由

Alireza Omidi¹, Jennifer M Bui¹, Jörg Gsponer¹

¹Michael Smith Laboratories, Department of Biochemistry & Molecular Biology, The University of British Columbia, Vancouver, BC, Canada.

|January 22, 2026

Abstract:

Two recent studies in Cell Systems show why protein dynamics matter for prediction. By moving beyond static structures and embracing the dynamic "jigglings and wigglings" that Richard Feynman famously described, these approaches improve accuracy in binding site predictions for flexible systems despite challenges such as sparse training data. Together, they signal a shift toward models that try to capture the full energy landscape, paving the way for deeper insights into protein function.

キーワード:

タンパク質相互作用部位予測 AlphaFold タンパク質ダイナミクス分子の柔軟性計算生物学

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Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans

Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans

Published on: November 26, 2017

A Protocol for Computer-Based Protein Structure and Function Prediction

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

関連する概念動画

Protein-protein Interfaces

Protein-protein Interfaces

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...

Protein-Protein Interfaces

Protein-Protein Interfaces

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

Predicting Molecular Geometry

Predicting Molecular Geometry

VSEPR Theory for Determination of Electron Pair Geometries

Protein Dynamics in Living Cells

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...