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Protein Folding

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Related Experiment Video

Updated: Feb 3, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

Monotopic Membrane Proteins Join the Fold.

Karen N Allen¹, Sonya Entova², Leah C Ray³

¹Department of Chemistry, Boston University, Boston, MA 02215, USA; Program in Biomolecular Pharmacology, Boston University School of Medicine, Boston, MA 02118, USA.

Trends in Biochemical Sciences

|October 20, 2018

Summary

This summary is machine-generated.

Monotopic membrane proteins, which embed into one side of cell membranes, have unique features. Recent studies reveal common characteristics and assembly strategies, offering insights into their function at membrane interfaces.

Keywords:

membrane interface membrane–protein interaction membranome monotopic enzymes

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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

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Area of Science:

Biochemistry
Structural Biology
Membrane Biology

Background:

Monotopic membrane proteins are proteins that associate with only one leaflet of the lipid bilayer.
These proteins are typically underrepresented in structural databases like the Protein Data Bank (PDB).
Recent research has identified new examples, enabling the characterization of their generalizable features.

Purpose of the Study:

To summarize the shared characteristics of monotopic membrane proteins.
To discuss their modes of membrane association and interaction mechanisms.
To explore their potential roles in cellular pathways and structure determination challenges.

Main Methods:

Review and synthesis of recent literature on monotopic membrane proteins.
Analysis of structural data and functional studies.
Comparative analysis of protein topology and homology.

Main Results:

Identified common features including oligomerization states and membrane association modes.
Described mechanisms for interacting with hydrophobic and amphiphilic substrates.
Highlighted homology to soluble protein folds.
Discussed the role of enzyme associations in metabolic pathways for specificity.

Conclusions:

Monotopic membrane proteins exhibit diverse yet generalizable characteristics.
Their study presents unique structural determination challenges but promises significant insights.
Understanding these proteins is crucial for comprehending biological processes at membrane interfaces.