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Related Concept Videos

Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Related Experiment Video

Updated: Jun 3, 2026

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)
08:14

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)

Published on: April 20, 2015

A folding pathway-dependent score to recognize membrane proteins.

Hamid Hadi-Alijanvand1, Maryam Rouhani, Elizabeth A Proctor

  • 1Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.

Plos One
|March 11, 2011
PubMed
Summary
This summary is machine-generated.

Predicting protein membrane localization is challenging. We developed FP(3)mem, a novel biophysical score derived from principal component analysis (PCA), to accurately forecast alpha-helical membrane protein localization.

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Last Updated: Jun 3, 2026

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)
08:14

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)

Published on: April 20, 2015

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

Area of Science:

  • Biophysics
  • Molecular Biology
  • Computational Biology

Background:

  • Accurately predicting protein localization, particularly membrane localization, remains a significant challenge in molecular biology.
  • Existing methods for studying protein localization often lack predictive power for specific membrane targeting.

Purpose of the Study:

  • To develop a mechanistic biophysical model for predicting the membrane localization propensity of alpha-helical membrane proteins.
  • To introduce a novel predictive score, FP(3)mem, based on protein folding pathways and biophysical parameters.

Main Methods:

  • Analysis of the folding pathway steps for alpha-helical membrane proteins.
  • Integration of biophysical parameters associated with each folding step.
  • Application of Principal Component Analysis (PCA) to identify key parameters driving membrane localization.
  • Development and validation of the FP(3)mem score.

Main Results:

  • A new score, FP(3)mem, was created to quantify the propensity of proteins for membrane localization.
  • The FP(3)mem score is derived from PCA of critical biophysical parameters.
  • FP(3)mem successfully rationalized the observed colocalization of several channel proteins with the Cav1.2 channel, attributing it to their lower membrane localization propensities.

Conclusions:

  • The FP(3)mem score offers a powerful new tool for predicting alpha-helical membrane protein localization.
  • This mechanistic approach provides insights into the biophysical basis of membrane targeting.
  • The findings have implications for understanding protein-protein interactions and cellular organization, particularly concerning ion channels.