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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Lipids as Anchors01:32

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
Membrane Fluidity01:26

Membrane Fluidity

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
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is a relatively...
Factors Affecting Protein-Drug Binding: Drug Interactions01:23

Factors Affecting Protein-Drug Binding: Drug Interactions

Drug interactions are a critical aspect of pharmacology and can occur when two or more drugs compete for the same binding site. This competition can result in one drug displacing another, altering the effect of the displaced drug. Drug interactions are complex processes that rely heavily on how much of the displacer drug is present and how strongly it can bind to the same sites as the displaced drug.
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions
04:45

Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions

Published on: February 10, 2022

Lipid-protein interactions.

Anthony G Lee1

  • 1School of Biological Sciences, Life Sciences Building, University of Southampton, U.K. agl@soton.ac.uk

Biochemical Society Transactions
|May 24, 2011
PubMed
Summary
This summary is machine-generated.

Intrinsic membrane proteins interact with surrounding annular and non-annular lipids. Hydrophobic matching and lipid headgroup structure influence binding, impacting protein function.

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Construction of Model Lipid Membranes Incorporating G-protein Coupled Receptors (GPCRs)

Published on: February 5, 2022

Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Biophysics

Background:

  • Intrinsic membrane proteins are surrounded by annular lipids, which interact with their membrane-spanning regions.
  • Non-annular lipids are found between transmembrane alpha-helices.
  • Lipid-protein interactions are crucial for membrane protein function and stability.

Purpose of the Study:

  • To investigate the factors influencing annular and non-annular lipid binding to membrane proteins.
  • To explore the relationship between lipid properties (chain length, headgroup) and binding constants.
  • To understand the role of hydrophobic matching and protein structure in lipid interactions.

Main Methods:

  • Analysis of annular lipid binding constants in relation to fatty acyl chain length.
  • Examination of the dependence of binding on lipid headgroup structure, including anionic lipids.
  • Consideration of models involving lipid bilayer distortion and transmembrane alpha-helical bundle distortion.
  • Investigating binding at non-annular sites, exemplified by the potassium channel KcsA.

Main Results:

  • Annular lipid binding constants show a dependence on fatty acyl chain length, but less than predicted by bilayer distortion models alone.
  • Hydrophobic matching between proteins and bilayers involves distortion of transmembrane alpha-helical bundles, affecting protein function.
  • Lipid headgroup structure significantly influences binding, with identified hotspots for anionic lipid binding.
  • Anionic lipid binding to non-annular sites, such as in KcsA, is functionally important.

Conclusions:

  • The packing preferences of membrane-spanning alpha-helices create a structure that favorably matches the surrounding lipid bilayer.
  • Lipid-protein interactions are optimized through a complementary fit, minimizing the need for significant structural changes in either component.
  • Understanding these interactions is key to deciphering membrane protein function and designing strategies for modulating their activity.