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Related Concept Videos

Membrane Fluidity01:23

Membrane Fluidity

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.Fatty acids tails of phospholipids can be either saturated or...
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Mosaic nature of the membrane
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Protein Dynamics in Living Cells

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Fluid Mosaic Model

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Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
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Published on: September 13, 2014

Hydration dynamics at fluorinated protein surfaces.

Oh-Hoon Kwon1, Tae Hyeon Yoo, Christina M Othon

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.

Proceedings of the National Academy of Sciences of the United States of America
|September 22, 2010
PubMed
Summary
This summary is machine-generated.

Surface fluorination of proteins slows water motion. This study reveals how fluorinated side chains create electrostatic drag, impacting protein dynamics and function by altering water interactions at the protein surface.

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Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
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In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS
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Fluorescence Recovery after Merging a Droplet to Measure the Two-dimensional Diffusion of a Phospholipid Monolayer
07:54

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Published on: October 15, 2015

Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Protein Science

Background:

  • Water-protein interactions are fundamental to protein function, influencing folding, dynamics, and catalysis.
  • Understanding these interactions is key to designing proteins with specific functions.

Purpose of the Study:

  • To investigate the impact of surface fluorination on water-protein interactions.
  • To systematically examine how side-chain volume and fluorination affect solvation dynamics.

Main Methods:

  • Modification of designed coiled-coil proteins with fluorinated amino acids (5,5,5-trifluoroleucine) or non-fluorinated analogs.
  • Utilizing ultrafast fluorescence spectroscopy to probe water dynamics at the protein surface.

Main Results:

  • Fluorinated side chains were successfully incorporated into designed proteins.
  • Ultrafast fluorescence spectroscopy revealed that fluorinated side chains significantly slow the motion of neighboring water molecules.
  • This effect is attributed to electrostatic drag exerted by the fluorinated groups.

Conclusions:

  • Surface fluorination alters water dynamics at the protein interface.
  • Fluorinated side chains can modulate protein solvation and potentially influence protein function through electrostatic effects on water.
  • This provides a novel approach to engineer protein behavior via surface modification.