In biochemistry and pharmacology, a ligand is a substance that forms a complex with a biomolecule to serve a biological purpose. The etymology stems from Latin ligare, which means 'to bind'. In protein-ligand binding, the ligand is usually a molecule which produces a signal by binding to a site on a target protein. The binding typically results in a change of conformational isomerism (conformation) of the target protein. In DNA-ligand binding studies, the ligand can be a small molecule, ion, or protein which binds to the DNA double helix. The relationship between ligand and binding partner is a function of charge, hydrophobicity, and molecular structure.
Binding occurs by intermolecular forces, such as ionic bonds, hydrogen bonds and Van der Waals forces. The association or docking is actually reversible through dissociation. Measurably irreversible covalent bonding between a ligand and target molecule is atypical in biological systems. In contrast to the definition of ligand in metalorganic and inorganic chemistry, in biochemistry it is ambiguous whether the ligand generally binds at a metal site, as is the case in hemoglobin. In general, the interpretation of ligand is contextual with regards to what sort of binding has been observed.
Ligand binding to a receptor protein alters the conformation by affecting the three-dimensional shape orientation. The conformation of a receptor protein composes the functional state. Ligands include substrates, inhibitors, activators, signaling lipids, and neurotransmitters. The rate of binding is called affinity, and this measurement typifies a tendency or strength of the effect. Binding affinity is actualized not only by host–guest interactions, but also by solvent effects that can play a dominant, steric role which drives non-covalent binding in solution. The solvent provides a chemical environment for the ligand and receptor to adapt, and thus accept or reject each other as partners.
Radioligands are radioisotope labeled compounds used in vivo as tracers in PET studies and for in vitro binding studies.
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In pharmacology, an inverse agonist is a drug that binds to the same receptor as an agonist but induces a pharmacological response opposite to that of the agonist. A neutral antagonist has no activity in the absence of an agonist or inverse agonist but can block the activity of either; they are in fact sometimes called blockers (examples include alpha blockers, beta blockers, and calcium channel blockers). Inverse agonists have opposite actions to those of agonists but the effects of both of these can be blocked by antagonists.
In biochemistry and pharmacology, a ligand is a substance that forms a complex with a biomolecule to serve a biological purpose. The etymology stems from Latin ligare, which means 'to bind'. In protein-ligand binding, the ligand is usually a molecule which produces a signal by binding to a site on a target protein. The binding typically results in a change of conformational isomerism (conformation) of the target protein. In DNA-ligand binding studies, the ligand can be a small molecule, ion, or protein which binds to the DNA double helix.
Efficacy is the ability to perform a task to a satisfactory or expected degree. The word comes from the same roots as effectiveness, and it has often been used synonymously, although in pharmacology a distinction is now often made between efficacy and effectiveness. The word efficacy is used in pharmacology and medicine to refer both to the maximum response achievable from a pharmaceutical drug in research settings, and to the capacity for sufficient therapeutic effect or beneficial change in clinical settings.
In this course we will study the cell (minimum unit of life) and its components. We will study several key cellular features: Membranes, genomes, channels and receptors. We will apply the laws of phys
This course covers the basic biophysical principles governing the thermodynamic and kinetic properties of biomacromolecules involved in chemical processes of life.
The course is held in English.
Presentation of selected signalling pathways with emphasis on both the mechanism of action of the molecules involved, molecular interactions and the role of their spatio-temporal organization within t
Covers selecting aptamers and binders based on binding affinities and additional properties for downstream testing.
Explores the design optimization of sensors and bioluminescent proteins for drug monitoring and metabolite visualization.
Explores oxidative addition, reductive elimination, insertion reactions, and factors influencing these reactions in organometallic chemistry.
G-protein-coupled receptors (GPCRs) are the largest class of cell surface receptors and drug targets, and respond to a wide variety of chemical stimuli to activate diverse cellular functions. Understa
bioRxiv2022
Transcription factor binding to a single binding site on DNA and its functional consequence in a promoter context are beginning to be relatively well understood. However, binding to clusters of sites
Strength in numbers, combining many weak interactions into an overall strong connection, is the fundamental principle of multivaleny. This concept has been exploiting for the engineering of super-sele