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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.
Mosaic nature of the membrane
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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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Enzyme Inhibition01:30

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Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
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Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
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Topoisomerases are enzymes that relax overwound DNA molecules during various cell processes, including DNA replication and transcription. These enzymes regulate positive and negative DNA supercoiling without changing the nucleotide sequence. DNA overwinding in a clockwise direction results in positively supercoiled DNA, whereas underwinding in a counterclockwise direction produces negatively supercoiled DNA.
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Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

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Disrupting enzyme fluidity.

Ganesh Srinivasan Anand1

  • 1Department of Chemistry and Huck Institute of Life Sciences, Pennsylvania State University, University Park, United States.

Elife
|January 25, 2021
PubMed
Summary
This summary is machine-generated.

Diverse small-molecule inhibitors were studied for their binding to Bruton

Keywords:
allosterybruton tyrosine kinasedrug resistancehydrogen/deuterium exchange mass spectrometrykinase inhibitormolecular biophysicsnonenuclear magnetic resonancestructural biology

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Area of Science:

  • Biochemistry and structural biology
  • Drug discovery and medicinal chemistry

Background:

  • Bruton's tyrosine kinase (BTK) is a crucial signaling molecule in B-cell development and function.
  • Dysregulation of BTK is implicated in various B-cell malignancies and autoimmune diseases.
  • Targeting BTK with small-molecule inhibitors is a validated therapeutic strategy.

Purpose of the Study:

  • To elucidate the structural mechanisms by which diverse small-molecule inhibitors interact with Bruton's tyrosine kinase.
  • To understand how these inhibitors induce conformational changes in the enzyme.
  • To provide insights for the rational design of novel and improved BTK inhibitors.

Main Methods:

  • Integration of X-ray crystallography for high-resolution structural determination.
  • Nuclear Magnetic Resonance (NMR) spectroscopy to probe dynamic interactions.
  • Mass spectrometry to analyze inhibitor binding and potential modifications.

Main Results:

  • Detailed structural insights into the binding modes of various small-molecule inhibitors.
  • Identification of distinct conformational states of Bruton's tyrosine kinase induced by different inhibitors.
  • Correlation between inhibitor structure, binding affinity, and observed conformational changes.

Conclusions:

  • The study reveals the complex structural interplay between small-molecule inhibitors and Bruton's tyrosine kinase.
  • Understanding these interactions is key to developing more selective and effective BTK-targeted therapies.
  • The findings contribute to the structural biology of kinase inhibition and drug design.