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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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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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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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The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
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Measurement of Force-Sensitive Protein Dynamics in Living Cells Using a Combination of Fluorescent Techniques
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Multidomain proteins under force.

Jessica Valle-Orero1, Jaime Andrés Rivas-Pardo, Ionel Popa

  • 1Department of Biological Sciences, Columbia University, New York, NY, United States of America.

Nanotechnology
|March 9, 2017
PubMed
Summary
This summary is machine-generated.

Single-molecule force spectroscopy reveals universal mechanical responses in proteins like titin, ubiquitin, and protein L. Force-induced unfolding and refolding steps normalize to a master curve, explained by polymer elasticity and energy landscape models.

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Area of Science:

  • Biophysics
  • Protein Mechanics
  • Polymer Physics

Background:

  • Single-molecule force spectroscopy (SMFS) techniques, including atomic force microscopy and magnetic tweezers, are crucial for understanding protein mechanics.
  • Investigating protein domain folding under force is essential for elucidating physiological roles.

Purpose of the Study:

  • To compare the mechanical responses of different protein folds (immunoglobulin-like and alpha+beta) under force.
  • To identify universal principles governing protein unfolding and refolding dynamics.

Main Methods:

  • Utilized SMFS (atomic force microscopy, magnetic tweezers) combined with protein engineering and HaloTag covalent attachment.
  • Studied four model proteins: I10, I91 (titin immunoglobulin domains), ubiquitin, and protein L (alpha+beta folds).

Main Results:

  • Proteins exhibited distinct mechanical responses and extensions under force.
  • Normalized unfolding and refolding force-step sizes collapsed onto a single master curve, independent of protein type.
  • This master curve aligns with predictions from polymer elasticity models, indicating an entropic contribution.

Conclusions:

  • A universal entropic mechanism governs force-induced domain transitions across different protein folds.
  • A combined protein folding and polymer physics energy landscape model accurately describes tandem domain behavior under force.
  • This model offers a valuable framework for analyzing complex multidomain proteins subjected to mechanical stress.