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Related Concept Videos

Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

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.
α-Helix containing multi-pass transmembrane proteins
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Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
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Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

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.
Protein Structure Is Critical to Its Biological Function
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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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Related Experiment Video

Updated: May 8, 2026

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

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

Published on: March 5, 2017

Helical membrane protein conformations and their environment.

Timothy A Cross1, Dylan T Murray, Anthony Watts

  • 1Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL, 32306, USA, cross@magnet.fsu.edu.

European Biophysics Journal : EBJ
|September 3, 2013
PubMed
Summary

Membrane proteins change shape and function based on their surroundings. Studying proteins in lipid bilayers, a native-like environment, reveals general principles of their environmental responses.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Membrane proteins function within cellular environments.
  • Previous structural studies often lacked native-like conditions.
  • Understanding environmental influence is crucial for membrane protein research.

Purpose of the Study:

  • To review the current understanding of membrane protein environmental responses.
  • To explore how lipid bilayers serve as native-like environments for structural studies.
  • To identify generic principles governing membrane protein behavior in lipid bilayers.

Main Methods:

  • Review of existing structural studies on membrane proteins.
  • Analysis of data from proteins embedded in lipid bilayers.
  • Comparison of responses in lipid versus non-lipid environments.

Main Results:

  • Growing evidence shows conformational and functional responses of membrane proteins to their environment.
  • Lipid bilayers provide a more native-like environment for structural characterization.
  • Studies reveal generic characteristics of protein responses to lipid environments.

Conclusions:

  • Structural insights from lipid bilayer-embedded proteins are vital.
  • These insights aid in refining models of membrane protein behavior.
  • Developing generic principles for model refinement is a key future direction.