| Chapter title |
Biophysical methods for identifying fragment-based inhibitors of protein-protein interactions.
|
|---|---|
| Chapter number | 39 |
| Book title |
Protein-Protein Interactions
|
| Published in |
Methods in molecular biology, January 2015
|
| DOI | 10.1007/978-1-4939-2425-7_39 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-2424-0, 978-1-4939-2425-7
|
| Authors |
Pfaff, Samuel J, Chimenti, Michael S, Kelly, Mark J S, Arkin, Michelle R, Samuel J. Pfaff, Michael S. Chimenti, Mark J. S. Kelly, Michelle R. Arkin, Pfaff, Samuel J., Chimenti, Michael S., Kelly, Mark J. S., Arkin, Michelle R. |
| Abstract |
Fragment-based lead discovery complements high-throughput screening and computer-aided drug design for the discovery of small-molecule inhibitors of protein-protein interactions. Fragments are molecules with molecular masses ca 280 Da or smaller, and are generally screened using structural or biophysical approaches. Several methods of fragment-based screening are feasible for any soluble protein that can be expressed and purified; specific techniques also have size limitations and/or require multiple milligrams of protein. This chapter describes some of the most common fragment-discovery methods, including surface plasmon resonance, nuclear magnetic resonance, differential scanning fluorimetry, and X-ray crystallography. |
Mendeley readers
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 20 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Researcher | 4 | 20% |
| Student > Ph. D. Student | 3 | 15% |
| Student > Doctoral Student | 2 | 10% |
| Student > Master | 2 | 10% |
| Student > Bachelor | 1 | 5% |
| Other | 1 | 5% |
| Unknown | 7 | 35% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 6 | 30% |
| Agricultural and Biological Sciences | 3 | 15% |
| Chemistry | 3 | 15% |
| Unknown | 8 | 40% |