Related Experiment Video
Updated: Jan 18, 2026

06:50
Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
Published on: January 26, 2024
2.5K
Factors controlling protein evolvability-at the molecular scale
1IMASL-CONICET, Universidad Nacional de San Luis, Ejército de Los Andes 950, San Luis, 5700, Argentina. jorgevila84@gmail.com.
European Biophysics Journal : EBJ
|January 17, 2026
Summary
No abstract available in PubMed .
Keywords:
Destabilizing mutationsEpistasisLeast action principleProtein pathwaysProtein robustnessProtein trajectoriesMore Related Videos
Related Concept Videos
Conservation of Protein Domains Over Different Proteins
14.1K
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...
14.1K
Protein Folding
126.4K
Overview
126.4K
Protein Folding
11.2K
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...
11.2K
Factors Affecting Protein-Drug Binding: Protein-Related Factors
524
Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
524
Covalently Linked Protein Regulators
8.7K
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....
These groups modify specific amino acids in a protein....
8.7K
Covalently Linked Protein Regulators
2.0K
2.0K

