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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
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 Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Ligand Binding Sites02:40

Ligand Binding Sites

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.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

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Related Experiment Video

Updated: Jun 4, 2026

Surface Passivation for Single-molecule Protein Studies
10:35

Surface Passivation for Single-molecule Protein Studies

Published on: April 24, 2014

Surface modification to control protein/surface interactions.

Lin Yuan1, Qian Yu, Dan Li

  • 1College of Chemistry, Chemical Engineering and Materials Science, Jiangsu Key Laboratory of Advanced Functional Polymer Design and Application, Soochow University, Suzhou, China.

Macromolecular Bioscience
|February 22, 2011
PubMed
Summary
This summary is machine-generated.

Controlling protein adsorption onto material surfaces is key for biomedical applications. Researchers are exploring surface chemistry and topography modifications to manage these crucial protein/surface interactions.

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Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
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Study of Short Peptide Adsorption on Solution Dispersed Inorganic Nanoparticles Using Depletion Method

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Last Updated: Jun 4, 2026

Surface Passivation for Single-molecule Protein Studies
10:35

Surface Passivation for Single-molecule Protein Studies

Published on: April 24, 2014

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
11:13

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

Study of Short Peptide Adsorption on Solution Dispersed Inorganic Nanoparticles Using Depletion Method
09:43

Study of Short Peptide Adsorption on Solution Dispersed Inorganic Nanoparticles Using Depletion Method

Published on: April 11, 2020

Area of Science:

  • Biomaterials Science
  • Surface Chemistry
  • Protein Adsorption

Background:

  • Protein/surface interactions are fundamental to biological processes and material biofunctionality.
  • Understanding and controlling these interactions is critical for developing effective biomedical materials.

Purpose of the Study:

  • To review methods for controlling protein adsorption via surface modification.
  • To highlight the role of chemical modification and surface topography.
  • To present future research perspectives in protein/surface interactions.

Main Methods:

  • Chemical modification of material surfaces.
  • Introduction of specific topographic features on surfaces.
  • Review of laboratory and published approaches.

Main Results:

  • Successful strategies for controlling protein adsorption have been identified.
  • Both surface chemistry and topography significantly influence protein adsorption.
  • The presented methods offer tunable control over protein-surface interactions.

Conclusions:

  • Tailoring surface properties is essential for managing protein adsorption.
  • Chemical and topographic modifications provide powerful tools for controlling bio-interactions.
  • Further research can advance the design of advanced biomaterials.