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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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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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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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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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Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
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Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich...
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Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy.

Evan S O'Brien1, Brian Fuglestad1,2, Henry J Lessen3

  • 1Department of Biochemistry & Biophysics, University of Pennsylvania, Perelman School of Medicine, Philadelphia, PA, 19104, USA.

Angewandte Chemie (International Ed. in English)
|April 12, 2020
PubMed
Summary
This summary is machine-generated.

Integral membrane proteins, sensory rhodopsin II and outer membrane protein W, exhibit fast side-chain dynamics. This high conformational entropy influences their function in lipid bilayers and detergent micelles.

Keywords:
NMR spectroscopyconformational entropymembrane proteinsprotein foldingside-chain dynamics

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Internal motions of integral membrane proteins are difficult to study experimentally.
  • Understanding protein dynamics is crucial for elucidating biological functions.

Purpose of the Study:

  • To characterize the fast side-chain dynamics of two integral membrane proteins: sensory rhodopsin II (α-helical) and outer membrane protein W (β-barrel).
  • To investigate how these dynamics differ or are similar in lipid bilayers versus detergent micelles.

Main Methods:

  • Solution Nuclear Magnetic Resonance (NMR) relaxation techniques were employed.
  • Methyl-bearing side-chain dynamics were analyzed in different membrane mimetics.

Main Results:

  • Both proteins showed similar distributions of methyl-bearing side-chain motion, irrespective of the membrane mimetic used.
  • Side chains in these membrane proteins are significantly more dynamic (ps-ns timescale) than those in soluble proteins.
  • High residual conformational entropy was observed in the folded state of these proteins.

Conclusions:

  • The observed dynamics and high conformational entropy in integral membrane proteins counterbalance the lack of a hydrophobic effect.
  • This conformational flexibility likely plays a significant role in membrane protein functions such as ligand binding, allostery, and signaling.