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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Membrane Proteins01:30

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Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
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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 cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell...
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Protein Transport into the Inner Mitochondrial Membrane01:34

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Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
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Translocation of Proteins into the Mitochondria01:19

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Intrinsic disorder in integral membrane proteins.

Brian J Aneskievich1, Rambon Shamilov2, Olga Vinogradova1

  • 1Department of Pharmaceutical Sciences, University of Connecticut, Storrs, CT, United States.

Progress in Molecular Biology and Translational Science
|October 17, 2021
PubMed
Summary

Integral membrane proteins (IMPs) may possess intrinsic disorder, challenging the classical lock-and-key model. Understanding this conformational flexibility is crucial for IMP function in health and disease.

Keywords:
Conformational dynamicsIntegral membrane protein (IMP)Intrinsically disordered protein (IDP)Intrinsically disordered region (IDR)Structural heterogeneity

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Medicine

Background:

  • Integral membrane proteins (IMPs) traditionally viewed via a lock-and-key model.
  • Emerging evidence highlights intrinsically disordered proteins (IDPs) and regions (IDRs) in complex protein structures.
  • This necessitates reevaluation of transmembrane protein conformation and function.

Purpose of the Study:

  • To explore the characteristics of IDPs and IDRs.
  • To investigate the functional advantages and disease-associated mutation impacts of intrinsic disorder in single-span IMPs.
  • To emphasize integrated approaches for studying disorder-containing IMPs.

Main Methods:

  • Review of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs).
  • Analysis of select single-span IMPs for functional advantages and mutation impacts.
  • Highlighting biophysical and computational methods for IMP investigation.
  • Stress on integrating in silico, in vitro, and in-cell assessments.

Main Results:

  • Intrinsic disorder may offer functional advantages to certain IMPs.
  • Disease-associated mutations can impact the conformational flexibility of IMPs.
  • Integrated biophysical, computational, and cellular methods are essential for comprehensive analysis.

Conclusions:

  • Intrinsic disorder in IMPs requires a shift from classical structural models.
  • Understanding IMP conformational flexibility is key to cellular physiology and disease.
  • Further research into disorder-containing IMPs can enhance their therapeutic potential.