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Related Concept Videos

Protein Folding01:25

Protein Folding

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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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Molecular Chaperones and Protein Folding03:00

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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...
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Membrane Fluidity01:26

Membrane Fluidity

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Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
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Mechanisms of Membrane Domain Formation00:59

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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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Multi-pass Transmembrane Proteins and β-barrels01:09

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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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Protein-protein Interfaces02:04

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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...
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Related Experiment Video

Updated: Aug 10, 2025

Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP
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Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP

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FkpA enhances membrane protein folding using an extensive interaction surface.

Taylor Devlin1, Dagan C Marx1, Michaela A Roskopf1

  • 1T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland, USA.

Protein Science : a Publication of the Protein Society
|February 13, 2023
PubMed
Summary

FkpA chaperone influences outer membrane protein (OMP) folding in gram-negative bacteria by increasing folded yield but decreasing folding rate. This chaperone utilizes an extensive binding interface for client interaction, requiring its full length for activity.

Keywords:
FkpAmembrane protein foldingouter membrane proteinouter membrane protein biogenesisperiplasmic chaperonephoto-crosslinkingsedimentation velocity

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

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

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Gram-negative bacteria rely on periplasmic chaperones like SurA, Skp, and FkpA for outer membrane protein (OMP) biogenesis.
  • These chaperones prevent aggregation and facilitate folding of unfolded OMPs (uOMPs).
  • FkpA's specific role in OMP folding, particularly under heat-shock stress, is less understood compared to other chaperones.

Purpose of the Study:

  • To elucidate the chaperone function of FkpA in the context of OMP folding.
  • To investigate how FkpA influences the folding rate and yield of OMPs.
  • To characterize the binding interaction between FkpA and unfolded OMPs.

Main Methods:

  • Monitoring the folding of three OMPs under FkpA influence.
  • Sedimentation velocity (SV) experiments to determine binding affinity and complex formation.
  • Photo-crosslinking experiments to map the FkpA-uOMP binding interface.
  • Utilizing subdomain constructs of FkpA to assess the role of its full length.

Main Results:

  • FkpA increases the folded yield but decreases the folding rate of OMPs, acting as a chaperone rather than a catalyst.
  • FkpA binds to all three tested unfolded OMPs with an affinity intermediate between Skp and SurA.
  • Complex formation is highly dependent on urea concentration, indicating an extensive binding interface spanning the entire FkpA molecule.
  • Full-length FkpA is essential for its complete chaperone activity.

Conclusions:

  • FkpA exerts a distinct and direct influence on OMP folding trajectory.
  • The chaperone activity of FkpA is mediated through a broad interaction interface with its clients.
  • Understanding FkpA's mechanism provides insights into the complex network of OMP biogenesis in bacteria.