Related Experiment Video
Updated: Mar 30, 2026
08:34
A Rapid and Quantitative Fluorimetric Method for Protein-Targeting Small Molecule Drug Screening
Published on: October 16, 2015
10.7K
Surface-Mediated Protein Unfolding as a Search Process for Denaturing Sites
James S Weltz1, Daniel K Schwartz1, Joel L Kaar1
1Department of Chemical and Biological Engineering, University of Colorado , Boulder, Colorado 80309, United States.
ACS Nano
|November 19, 2015
Summary
Protein unfolding on surfaces like fused silica is driven by diffusion to rare, nanoscale denaturing sites. This discovery aids in designing protein-compatible materials.
Area of Science:
- Biomaterials Science
- Surface Chemistry
- Protein Biophysics
Background:
- Surface-induced protein denaturation impacts biomaterial development.
- Understanding protein unfolding mechanisms at interfaces is crucial for material design.
Purpose of the Study:
- To elucidate the mechanism of lysozyme unfolding on fused silica surfaces.
- To investigate the role of surface interactions in protein denaturation.
Main Methods:
- Utilized single-molecule Förster resonance energy transfer (FRET) to monitor protein unfolding.
- Simultaneously tracked individual lysozyme molecule adsorption, diffusion, and desorption dynamics at the solid-solution interface.
- Employed high-throughput single-molecule analysis.
Main Results:
- Lysozyme unfolding on fused silica is mediated by surface diffusion.
- Denaturation occurs at specific, isolated nanoscale sites, not uniformly across the surface.
- These denaturing sites are rare and distinct from the bulk surface.
Conclusions:
- Protein unfolding at surfaces is an active search process for denaturing sites.
- Surface diffusion plays a key role in mediating protein denaturation.
- Findings inform the rational design of protein-compatible surfaces for various applications.
Keywords:
Förster resonance energy transferinterfacial protein diffusionparticle adsorptionprotein−surface interactionssingle-molecule trackingsurface heterogeneitytotal internal reflection fluorescence microscopyMore Related Videos
Related Concept Videos
01:28Protein Denaturation
10.7K
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
10.7K
03:00Molecular Chaperones and Protein Folding
20.8K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
20.8K
01:25Protein Folding
12.5K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
12.5K
01:22Protein Folding
36.5K
36.5K
01:22Protein Folding
130.5K
Overview
130.5K
00:49Ligand Binding and Linkage
6.0K
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...
6.0K