Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1994-6-9
|
| pubmed:abstractText |
A new semi-empirical method for calculating free energies of binding from molecular dynamics (MD) simulations is presented. It is based on standard thermodynamic cycles and on a linear approximation of polar and non-polar free energy contributions from the corresponding MD averages. The method is tested on a set of endothiapepsin inhibitors and found to give accurate results both for absolute as well as relative free energies.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0269-2139
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
7
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
385-91
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:8177887-Aspartic Acid Endopeptidases,
pubmed-meshheading:8177887-Binding Sites,
pubmed-meshheading:8177887-Computer Simulation,
pubmed-meshheading:8177887-Drug Design,
pubmed-meshheading:8177887-Electrochemistry,
pubmed-meshheading:8177887-Molecular Structure,
pubmed-meshheading:8177887-Protein Binding,
pubmed-meshheading:8177887-Thermodynamics
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
A new method for predicting binding affinity in computer-aided drug design.
|
| pubmed:affiliation |
Department of Molecular Biology, Uppsala University, Sweden.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|