Related Experiment Video
Updated: Mar 28, 2026
09:25
Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
Published on: November 1, 2024
3.0K
De Novo Proteins with Life-Sustaining Functions Are Structurally Dynamic
Grant S Murphy1, Jack B Greisman1, Michael H Hecht1
1Department of Chemistry, Princeton University, Princeton, NJ 08540, USA.
Journal of Molecular Biology
|December 29, 2015
Summary
Novel de novo proteins (SynRescue) can rescue essential gene mutations in bacteria, even without forming highly ordered structures. This suggests dynamic protein structures may be crucial for early life functions.
Area of Science:
- Synthetic biology
- Protein engineering
- Structural biology
Background:
- Designing novel proteins with specific functions is a major goal in synthetic biology.
- A library of de novo proteins was created to fold into 4-helix bundles.
- Previous work identified de novo protein sequences (SynRescue) that rescue essential gene mutations in E. coli.
Purpose of the Study:
- Investigate the structural requirements for auxotroph rescue by SynRescue proteins.
- Understand the biophysical properties of SynRescue proteins.
Main Methods:
- Computational and experimental approaches were used.
- Circular dichroism, size-exclusion chromatography, and NMR spectroscopy were employed.
- Analysis of protein structure and dynamics.
Main Results:
- SynRescue proteins are alpha-helical and stable.
- These proteins do not form well-ordered structures.
- SynRescue proteins exhibit dynamic structures, fluctuating between monomeric and dimeric states.
Conclusions:
- Well-ordered protein structure is not essential for life-sustaining functions.
- Dynamic protein structures may have played a significant role in the early evolution of protein function.
Related Concept Videos
01:56Structural Protein Function
3.4K
3.4K
01:56Structural Protein Function
30.5K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
30.5K
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
130.4K
Overview
130.4K
01:22Protein Folding
36.5K
36.5K
01:57Protein Complexes with Interchangeable Parts
3.1K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
3.1K