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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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Physiological pharmacokinetic models, often called flow-limited or perfusion models, typically assume a swift drug distribution between tissue and venous blood, creating a rapid drug equilibrium. This premise is based on the idea that drug diffusion is extremely fast, and the cell membrane presents no barrier to drug permeation. In this scenario, where no drug binding occurs, the drug concentration in the tissue equals that of the venous blood leaving the tissue. This greatly simplifies the...
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Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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Diffusion is the passive movement of substances down their concentration gradients—requiring no expenditure of cellular energy. Substances, such as molecules or ions, diffuse from an area of high concentration to an area of low concentration in the cytosol or across membranes. Eventually, the concentration will even out, with the substance moving randomly but causing no net change in concentration. Such a state is called dynamic equilibrium, which is essential for maintaining overall...
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Diffusion is a type of passive transport. In passive transport, a substance tends to move from an area of high concentration to an area of low concentration until the concentration is equal across the space. For example, take the diffusion of substances through the air. When someone opens a perfume bottle in a room filled with people, the perfume is at its highest concentration in the bottle and is at its lowest at the edges of the room. The perfume vapor will diffuse, or spread away, from the...
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Diffusion-limited association of disordered protein by non-native electrostatic interactions.

Jae-Yeol Kim1, Fanjie Meng1, Janghyun Yoo1

  • 1Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892-0520, USA.

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Intrinsically disordered proteins (IDPs) fold upon binding. This study reveals their transient complexes (TCs) are stabilized by electrostatic interactions, with significantly longer lifetimes than folded proteins, aiding IDP folding during binding.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Intrinsically disordered proteins (IDPs) often fold upon binding to their targets.
  • This coupled binding and folding process is complex and differs from interactions between already folded proteins.
  • Understanding the transient complex (TC) formation is key, but experimentally challenging due to its short lifespan.

Purpose of the Study:

  • To investigate the mechanism of coupled binding and folding in IDPs.
  • To analyze the role and characteristics of the transient complex (TC) during IDP association.
  • To determine factors influencing the association rate and TC stability.

Main Methods:

  • Utilized single-molecule fluorescence spectroscopy.
  • Investigated the diffusion-limited association mechanism of an IDP.
  • Performed photon-by-photon analysis to characterize TC dynamics.

Main Results:

  • Observed a significant enhancement in the association rate of the IDP.
  • Identified stabilization of the TC by non-native electrostatic interactions.
  • Found TC lifetimes for IDP binding to be at least two orders of magnitude longer than for folded protein binding.

Conclusions:

  • The long lifetime of the transient complex (TC) appears generally necessary for the folding of intrinsically disordered proteins (IDPs) during the binding process.
  • Non-native electrostatic interactions play a crucial role in stabilizing TCs and enhancing association rates.
  • Single-molecule spectroscopy provides valuable insights into the dynamics of IDP interactions.