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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 polypeptide...

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Related Experiment Video

Updated: May 25, 2026

Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions

Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions

Published on: February 10, 2022

Emerging methodologies to investigate lipid-protein interactions.

Jordan L Scott¹, Catherine A Musselman, Emmanuel Adu-Gyamfi

¹Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.

Integrative Biology : Quantitative Biosciences From Nano to Macro

|February 14, 2012

Summary

Peripheral proteins bind lipids to regulate cellular functions. New tools and integrated approaches are crucial for understanding these vital protein-lipid interactions in cell signaling and membrane trafficking.

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Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction

Published on: April 26, 2011

Related Experiment Videos

Last Updated: May 25, 2026

Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions

Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions

Published on: February 10, 2022

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction

Published on: April 26, 2011

Area of Science:

Cell Biology
Biochemistry
Molecular Biology

Background:

Cellular membranes utilize hundreds of lipids, channels, and receptors as signaling platforms.
Peripheral proteins reversibly interact with membrane lipids, mediated by specific lipid-binding domains, to regulate cellular processes.
Understanding these protein-lipid interactions is key to cellular signaling and trafficking.

Purpose of the Study:

To review emerging cellular and in vitro methods for studying protein-lipid interactions.
To provide perspective on integrating diverse technologies for a comprehensive understanding of lipid signaling.
To highlight the need for novel, sensitive, and quantitative tools in this field.

Main Methods:

Survey of emerging cellular and in vitro approaches.
Discussion of traditional in vitro and in vivo studies.
Integration of computational biology, lipid mapping, single-molecule imaging, and lipidomics.

Main Results:

Identification of over 10 modular lipid-binding domains since 1989, each with structurally selective lipid-binding sites.
Elucidation of how these domains coordinate lipids, influencing protein-membrane association.
Demonstration that protein-lipid binding affinities and selectivity dictate cellular activities and physiological outcomes.

Conclusions:

Novel tools and integrated methodologies are essential for advancing the study of protein-lipid interactions.
Future research should focus on integrating diverse technologies to detail molecular architecture and mechanisms of lipid signaling.
Continued exploration of protein-lipid interactions will deepen our understanding of fundamental cellular processes.