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Related Concept Videos

Solvents01:12

Solvents

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A solvent is a substance, most often a liquid, that can dissolve other substances. Here, the substance being dissolved is called a solute. When a solvent and a solute combine, they form a solution - a homogenous mixture of both the solvent and the solute. Water is a universal biological solvent. Its polar structure allows it to dissolve many other polar compounds. The ability of water to dissolve is governed by a balance between water molecules binding to each other and binding to the solute.
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Channel Rhodopsins01:11

Channel Rhodopsins

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Most organisms use photoreceptors to sense and respond to light. Examples of photoreceptors include bacteriorhodopsins and bacteriophytochromes in some bacteria, phytochromes in plants, and rhodopsins in the photoreceptor cells of the vertebral retina. The light-sensitive property of these receptors is because of the bound chromophores, such as bilin in the phytochromes and retinal in the rhodopsins.
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Ligand Binding Sites02:40

Ligand Binding Sites

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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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Metal-Ligand Bonds02:51

Metal-Ligand Bonds

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The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
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Titration in Nonaqueous Solvents01:16

Titration in Nonaqueous Solvents

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Most acid-base titrations are performed in an aqueous medium. In aqueous titrations, water competes with weaker acids or bases for proton donation or acceptance, leading to ambiguous endpoints in the titration curve. Water also affects the partial ionization of weak acids or bases. For example, water accepts a proton from acetic acid to form hydronium and acetate ions. The hydronium ion formed is a stronger acid than acetic acid, and the acetate ion is a stronger base than water. As a result,...
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Removal and Replacement of Endogenous Ligands from Lipid-Bound Proteins and Allergens
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Removal and Replacement of Endogenous Ligands from Lipid-Bound Proteins and Allergens

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Lipids Alter Rhodopsin Function via Ligand-like and Solvent-like Interactions.

Leslie A Salas-Estrada1, Nicholas Leioatts2, Tod D Romo3

  • 1Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, New York.

Biophysical Journal
|February 6, 2018
PubMed
Summary

Rhodopsin

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Area of Science:

  • Membrane protein structure and function
  • Photoreceptor biology
  • Biophysics of G protein-coupled receptors

Background:

  • Rhodopsin, a G protein-coupled receptor (GPCR), senses light but its functional modulation by lipid environment is unclear.
  • Two hypotheses exist: solvent-like lipid interactions or ligand-like protein-lipid interactions.
  • Understanding these mechanisms is key to rhodopsin's function and stability.

Purpose of the Study:

  • Investigate molecular mechanisms of lipid modulation on rhodopsin.
  • Differentiate between solvent-like and ligand-like interaction hypotheses.
  • Elucidate how lipid composition affects rhodopsin's structure and function.

Main Methods:

  • All-atom molecular dynamics simulations.
  • Analysis of five distinct rhodopsin states.
  • Computational modeling of protein-lipid interactions.

Main Results:

  • Receptor activation induces local ordering in the membrane.
  • Specific lipids, like docosahexaenoic acid (DHA) and phosphatidylethanolamine (PE), act as weak ligands.
  • These lipids preferentially bind to inactive rhodopsin conformations, causing structural changes.

Conclusions:

  • Protein-lipid interactions in rhodopsin are ligand-like, not purely solvent-like.
  • Specific lipid binding modulates rhodopsin conformation and stability.
  • Findings provide molecular insights into GPCR-lipid interactions.