Related Experiment Video
Updated: Jun 6, 2025
09:01
Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli
Published on: March 16, 2011
30.4K
Corrigendum: Camel proteins and enzymes: a growing resource for functional evolution and environmental adaptation
Mahmoud Kandeel1,2, Abdulla Al-Taher1, Katharigatta N Venugopala3,4
1Department of Biomedical Sciences, College of Veterinary Medicine, King Faisal University, Al-Ahsa, Saudi Arabia.
Frontiers in Veterinary Science
|November 22, 2024
Summary
This study corrects a previous article DOI. The corrected DOI ensures proper citation and access to the research findings for veterinarians and researchers.
Area of Science:
- Veterinary Science
- Animal Health
- Comparative Medicine
Context:
- Ensuring accurate scientific record-keeping is crucial for research integrity.
- Proper citation facilitates knowledge sharing and reproducibility in veterinary medicine.
Purpose:
- To correct the Digital Object Identifier (DOI) for a previously published article.
- To rectify any potential issues with accessing or citing the research.
Summary:
- The article DOI has been corrected to ensure accurate referencing.
- This correction facilitates the retrieval of scientific information within veterinary research.
Impact:
- Improves the accuracy of the scientific literature.
- Enhances the accessibility of research findings for the veterinary community.
Related Concept Videos
01:07Catalytically Perfect Enzymes
3.9K
The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
Most enzymes...
Most enzymes...
3.9K
02:26Conservation of Protein Domains Over Different Proteins
10.8K
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
10.8K
01:19Allosteric Proteins-ATCase
5.7K
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
5.7K
01:57Adaptations that Reduce Water Loss
25.1K
Though evaporation from plant leaves drives transpiration, it also results in loss of water. Because water is critical for photosynthetic reactions and other cellular processes, evolutionary pressures on plants in different environments have driven the acquisition of adaptations that reduce water loss.
25.1K
00:49Ligand Binding and Linkage
4.8K
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...
4.8K
01:18Amino Acid Catabolism
1
Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
1