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Related Concept Videos

Amino acids03:42

Amino acids

Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...
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 Lipids01:32

Membrane Lipids

Lipids are an essential component of all biological membranes. The average lipid content in mammalian membranes is 50%, though it can be as low as 20% in the inner mitochondrial membrane or as high as 80% in the myelin sheath present around the nerve cells.
Phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, and sphingomyelin are the most common phospholipids present in mammalian membranes. At physiological pH, phosphatidylserine is negatively charged, while the other three...
Membrane Lipids01:32

Membrane Lipids

Lipids are an essential component of all biological membranes. The average lipid content in mammalian membranes is 50%, though it can be as low as 20% in the inner mitochondrial membrane or as high as 80% in the myelin sheath present around the nerve cells.
Phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, and sphingomyelin are the most common phospholipids present in mammalian membranes. At physiological pH, phosphatidylserine is negatively charged, while the other three...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

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...
Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...

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Related Experiment Video

Updated: Jul 10, 2026

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
07:02

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy

Published on: December 16, 2021

Is arginine charged in a membrane?

Libo Li, Igor Vorobyov, Alexander D MacKerell

    Biophysical Journal
    |November 6, 2007
    PubMed
    Summary

    Charged amino acids like arginine (Arg) face high energy barriers when exposed to lipid membranes. This challenges existing models and impacts understanding of protein function in membranes.

    Area of Science:

    • Biophysics
    • Molecular Biology
    • Membrane Protein Dynamics

    Background:

    • Charged amino acids are crucial for protein structure and function.
    • Their behavior at membrane interfaces is not fully understood, with recent models suggesting low energy penalties for exposure to lipids, contrary to established views.

    Discussion:

    • This study quantifies the free energy landscape for a lipid-exposed arginine residue across a membrane using computational models.
    • It investigates the influence of protonation state and membrane interactions on arginine's behavior.

    Key Insights:

    • High free energy barriers exist for both charged and neutral arginine states exposed to lipids.
    • Membrane deformations stabilize the protonated form, causing a significant pK(a) shift (≤4.5 units), keeping arginine mostly protonated.

    More Related Videos

    Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.
    11:10

    Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.

    Published on: April 5, 2018

    Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
    09:49

    Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

    Published on: April 2, 2015

    Related Experiment Videos

    Last Updated: Jul 10, 2026

    Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
    07:02

    Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy

    Published on: December 16, 2021

    Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.
    11:10

    Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.

    Published on: April 5, 2018

    Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
    09:49

    Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

    Published on: April 2, 2015

  • The energetic cost of exposing arginine to lipid hydrocarbon is substantial.

    • Outlook:

    • Findings have implications for understanding membrane translocation processes.
    • This work refines models of voltage-gated ion channel activation and other membrane protein functions.