| Chapter title |
Molecular Dynamics Studies of Matrix Metalloproteases
|
|---|---|
| Chapter number | 7 |
| Book title |
Matrix Metalloproteases
|
| Published in |
Methods in molecular biology, March 2017
|
| DOI | 10.1007/978-1-4939-6863-3_7 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-6861-9, 978-1-4939-6863-3
|
| Authors |
Natalia Díaz, Dimas Suárez |
| Editors |
Charles A. Galea |
| Abstract |
Matrix metalloproteases are multidomain enzymes with a remarkable proteolytic activity located in the extracellular environment. Their catalytic activity and structural properties have been intensively studied during the last few decades using both experimental and theoretical approaches, but many open questions still remain. Extensive molecular dynamics simulations enable the sampling of the configurational space of a molecular system, thus contributing to the characterization of the structure, dynamics, and ligand binding properties of a particular MMP. Based on previous computational experience, we provide in this chapter technical and methodological guidelines that may be useful to and stimulate other researchers to perform molecular dynamics simulations to help address unresolved questions concerning the molecular mode of action of MMPs. |
Mendeley readers
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 5 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 2 | 40% |
| Student > Bachelor | 1 | 20% |
| Researcher | 1 | 20% |
| Unknown | 1 | 20% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 3 | 60% |
| Materials Science | 1 | 20% |
| Unknown | 1 | 20% |