Related Experiment Video
Updated: May 5, 2026
15:06
Synthesis of an Intein-mediated Artificial Protein Hydrogel
Published on: January 27, 2014
11.6K
Naturally split inteins assemble through a "capture and collapse" mechanism.
Neel H Shah1, Ertan Eryilmaz, David Cowburn
1Department of Chemistry, Princeton University , Frick Laboratory, Princeton, New Jersey 08544, United States.
Journal of the American Chemical Society
|November 19, 2013
Summary
Split inteins achieve their unique structure through a novel mechanism where disordered fragments bind and form an ordered intermediate before folding. This finding advances protein engineering technologies.
Area of Science:
- Biochemistry
- Protein Engineering
- Molecular Biology
Background:
- Split inteins are proteins that perform protein splicing in trans.
- Their molecular recognition and assembly mechanism remain unclear.
- Split intein chemistry is crucial for protein engineering.
Purpose of the Study:
- To elucidate the mechanism of split intein fragment association and assembly.
- To understand how the unique topology is achieved upon binding.
- To provide insights for advancing split intein-based technologies.
Main Methods:
- Biophysical techniques
- Protein engineering methods
- Segmental isotopic labeling
Main Results:
- One split intein fragment is partly folded, the other is disordered.
- Disordered regions mediate binding and form an ordered intermediate.
- This intermediate then collapses into the native intein fold.
Conclusions:
- A novel mechanism for split intein assembly involving disordered regions has been identified.
- Understanding this mechanism enhances knowledge of protein folding and molecular recognition.
- This research will improve the development and application of split intein technologies.
Related Concept Videos
01:32RNA Splicing
53.5K
Splicing is the process by which eukaryotic RNA is edited before its translation into protein. The RNA strand transcribed from eukaryotic DNA is called the primary transcript. The primary transcripts that become mRNAs are called precursor messenger RNAs (pre-mRNAs). Eukaryotic pre-mRNA contains alternating sequences of exons and introns. Exons are nucleotide sequences that code for proteins, whereas introns are the non-coding regions. In RNA splicing, introns are removed and exons are bonded...
53.5K
01:15Activation of Integrins
4.4K
Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
4.4K
01:35Disassembly of Intermediate Filaments
2.0K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
2.0K
01:02Protein Digestion
86.5K
Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
86.5K
01:19Translocation of Proteins into the Mitochondria
8.8K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
8.8K
01:38Intralumenal Vesicles and Multivesicular Bodies
4.0K
Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
4.0K