Fragment-Based Drug Discovery: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 17: Line 17:
! scope="col" width="5000px" | SAR by NMR
! scope="col" width="5000px" | SAR by NMR
|-  
|-  
| scope="col" width="5000px" | Structure-activity relationship (SAR) by NMR is one tool that can be used to design and develop new drugs. This is the process "in which small organic molecules that bind to proximal subsites of a protein are identified, optimized, and linked together to produce high-affinity ligands."<ref name="Shuker S. B., Hajduk P. J., Meadows R. P., Fesik S. W. Discovering High-Affinity Ligands for Proteins: SAR by NMR. Science; Nov 29, 1996; 274, 5292; ProQuest Central pg. 1531.">Shuker S. B., Hajduk P. J., Meadows R. P., Fesik S. W. Discovering High-Affinity Ligands for Proteins: SAR by NMR. Science; Nov 29, 1996; 274, 5292; ProQuest Central pg. 1531.</ref> In other words, NMR is used to identify the components responsible for binding and analyze the relationship between the ligand and the biological target.
| scope="col" width="5000px" | Structure-activity relationship (SAR) by NMR is one tool that can be used to design and develop new drugs. This is the process in which NMR is used to identify the components responsible for binding to the protein. NMR is also used to analyze the relationships between these components to determine where the protein binding sites are located and how the ligand interacts with those sites.<ref name="Shuker S. B., Hajduk P. J., Meadows R. P., Fesik S. W. Discovering High-Affinity Ligands for Proteins: SAR by NMR. Science; Nov 29, 1996; 274, 5292; ProQuest Central pg. 1531.">Shuker S. B., Hajduk P. J., Meadows R. P., Fesik S. W. Discovering High-Affinity Ligands for Proteins: SAR by NMR. Science; Nov 29, 1996; 274, 5292; ProQuest Central pg. 1531.</ref>
|}
|}