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Related Concept Videos

Cell-surface Signaling01:21

Cell-surface Signaling

54.7K
Hormones—or any molecule that binds to a receptor, known as a ligand—that are lipid-insoluble (water-soluble) are not able to diffuse across the cell membrane. In order to be able to affect a cell without entering it, these hormones bind to receptors on the cell membrane. When a first messenger, a hormone, binds to a receptor, a signal cascade is set off, causing second messengers, proteins inside the cell, to become activated, resulting in downstream effects.
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Types of Receptors: Cell Surface Receptors01:28

Types of Receptors: Cell Surface Receptors

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Cell-surface receptors, also known as transmembrane receptors, are cell surface, membrane-anchored (integral) proteins that bind to external ligand molecules. This type of receptor spans the plasma membrane and performs signal transduction, converting an extracellular signal into an intracellular signal. Ligands that interact with cell-surface receptors do not have to enter the cell that they affect. Cell-surface receptors are also called cell-specific proteins or markers because they are...
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Surface Tension and Surface Energy01:16

Surface Tension and Surface Energy

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When a paint brush is immersed in water, the bristles wave freely inside the water. When it is taken out, the bristles stick together. The reason behind this effect is surface tension.
Consider a beaker filled with liquid. The bulk molecules in the liquid experience equal attractive forces on all sides with the surrounding molecules. However, the surface molecules experience a net attractive force downward due to the bulk molecules. The surface of the liquid behaves like a stretched membrane,...
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Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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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...
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Wood Surfacing01:14

Wood Surfacing

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Wood surfacing is a critical finishing process designed to smoothen the wood surface, enhance its dimensional accuracy, and make handling safer. This process compensates for potential shrinkage during the seasoning phase by marginally increasing the wood dimensions before surfacing. It also helps correct some distortions that may occur as the wood dries.
The equipment used in the surfacing process is a plane equipped with rotating blades. This tool efficiently smoothens the wood surface and can...
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Related Experiment Video

Updated: Feb 13, 2026

Purification of Biotinylated Cell Surface Proteins from Rhipicephalus microplus Epithelial Gut Cells
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Purification of Biotinylated Cell Surface Proteins from Rhipicephalus microplus Epithelial Gut Cells

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Biotinylation of Cell Surface Proteins.

Guo N Huang1

  • 1Program in Biochemistry, Cellular and Molecular Biology, Johns Hopkins University School of Medicine, Baltimore, USA.

Bio-Protocol
|March 20, 2018
PubMed
Summary

This protocol biochemically labels and separates plasma membrane proteins, enabling study of their dynamic interactions. It facilitates analysis of cell surface protein signaling and regulation.

Area of Science:

  • Cellular Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Membrane proteins are crucial for sensing external signals and initiating intracellular communication.
  • Cell surface membrane protein abundance is dynamically regulated, independent of total cellular levels.
  • Understanding these dynamic changes is key to deciphering cellular signaling pathways.

Purpose of the Study:

  • To present a protocol for biochemically labeling and separating plasma membrane proteins.
  • To enable the study of dynamic interactions involving cell surface membrane proteins.
  • To facilitate functional analysis of membrane protein interactions with other cellular components.

Main Methods:

  • Biochemical labeling of membrane proteins.
  • Separation of plasma membrane proteins from intracellular compartments.

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Determining Cell-surface Expression and Endocytic Rate of Proteins in Primary Astrocyte Cultures Using Biotinylation
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Determining Cell-surface Expression and Endocytic Rate of Proteins in Primary Astrocyte Cultures Using Biotinylation

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Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions
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Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

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Related Experiment Videos

Last Updated: Feb 13, 2026

Purification of Biotinylated Cell Surface Proteins from Rhipicephalus microplus Epithelial Gut Cells
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Determining Cell-surface Expression and Endocytic Rate of Proteins in Primary Astrocyte Cultures Using Biotinylation
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Determining Cell-surface Expression and Endocytic Rate of Proteins in Primary Astrocyte Cultures Using Biotinylation

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Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions
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  • Co-immunoprecipitation and western blot analysis.

    • Main Results:

    • Successful isolation and biochemical characterization of plasma membrane proteins.
    • Demonstration of the protocol's utility in analyzing dynamic protein interactions.
    • Validation of the method for studying cell surface protein regulation.

    Conclusions:

    • The developed protocol effectively distinguishes and isolates plasma membrane proteins.
    • This method allows for detailed functional analysis of dynamic membrane protein interactions.
    • The protocol provides a valuable tool for investigating cell surface signaling and regulation.