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Protein ligand interactions
● A protein ligand is an atom, a molecule or an
ion which can bind to a specific site (the binding
site) on a protein.
● AKA affinity reagents or protein binders.
● To date, antibodies are the most widely used
protein ligands in life-science investigations
● Other molecules such as, nucleic acids,
peptides are also being used.
● Main methods to study protein–ligand interactions are principal
hydrodynamic and calorimetric techniques, and principal spectroscopic
and structural methods such as
1. Fourier transform spectroscopy
2. Raman spectroscopy
3. Fluorescence spectroscopy
4. Circular dichroism
5. Nuclear magnetic resonance
6. Mass spectrometry
7. Atomic force microscope
8. Paramagnetic probes
9. Dual Polarisation Interferometry
● Molecular recognition via protein–ligand interactions is of
fundamental importance to most processes occurring within
living organisms.
● Transmission of signals via molecular complementarity is
essential to all life processes.
● The evolution of protein function includes the development of
highly specific sites for the binding of ligands with affinities
tailored to meet the needs of biological function.
● Cooperativity in ligand binding plays an important role in
the regulation of biological function.
● Cooperativity in ligand binding is linked to conformational
change in the protein.
● Well‐defined mathematical expressions based on the
stoichiometry of the binding equilibrium provide a means
for quantifying ligand‐binding interactions.
●
The equilibrium constants of ligand–macromolecule interactions
provide a thermodynamic measure of the strength of the
interaction.
● The atomic resolution structures of ligand complexes provide a
chemical basis for understanding protein–ligand interactions and
these structures are often used as the basis for the design of
small‐molecule drugs for the treatment of disease.
●
The equilibrium constants of ligand–macromolecule interactions
provide a thermodynamic measure of the strength of the
interaction.
● The atomic resolution structures of ligand complexes provide a
chemical basis for understanding protein–ligand interactions and
these structures are often used as the basis for the design of
small‐molecule drugs for the treatment of disease.

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8.protein ligand interactions

  • 2. ● A protein ligand is an atom, a molecule or an ion which can bind to a specific site (the binding site) on a protein. ● AKA affinity reagents or protein binders. ● To date, antibodies are the most widely used protein ligands in life-science investigations ● Other molecules such as, nucleic acids, peptides are also being used.
  • 3. ● Main methods to study protein–ligand interactions are principal hydrodynamic and calorimetric techniques, and principal spectroscopic and structural methods such as 1. Fourier transform spectroscopy 2. Raman spectroscopy 3. Fluorescence spectroscopy 4. Circular dichroism 5. Nuclear magnetic resonance 6. Mass spectrometry 7. Atomic force microscope 8. Paramagnetic probes 9. Dual Polarisation Interferometry
  • 4. ● Molecular recognition via protein–ligand interactions is of fundamental importance to most processes occurring within living organisms. ● Transmission of signals via molecular complementarity is essential to all life processes. ● The evolution of protein function includes the development of highly specific sites for the binding of ligands with affinities tailored to meet the needs of biological function.
  • 5. ● Cooperativity in ligand binding plays an important role in the regulation of biological function. ● Cooperativity in ligand binding is linked to conformational change in the protein. ● Well‐defined mathematical expressions based on the stoichiometry of the binding equilibrium provide a means for quantifying ligand‐binding interactions.
  • 6. ● The equilibrium constants of ligand–macromolecule interactions provide a thermodynamic measure of the strength of the interaction. ● The atomic resolution structures of ligand complexes provide a chemical basis for understanding protein–ligand interactions and these structures are often used as the basis for the design of small‐molecule drugs for the treatment of disease.
  • 7. ● The equilibrium constants of ligand–macromolecule interactions provide a thermodynamic measure of the strength of the interaction. ● The atomic resolution structures of ligand complexes provide a chemical basis for understanding protein–ligand interactions and these structures are often used as the basis for the design of small‐molecule drugs for the treatment of disease.