http://rdf.ncbi.nlm.nih.gov/pubchem/patent/KR-20160128882-A
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_d9e7f4e61481ea3b18f0a4bc21fafa10 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N33-68 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G06F19-16 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G06F19-16 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-68 |
| filingDate | 2015-09-25-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_43220dd57b8e25c864ce17c82c1f8c71 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_e3bcf5316996e635a0977848317ccb95 |
| publicationDate | 2016-11-08-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | KR-20160128882-A |
| titleOfInvention | Protein stability analysis method using protein folding thermodynamic |
| abstract | The present invention relates to a conformational entropy measurement method for a biomolecule, a free energy measurement method for a biomolecule, and a free energy difference measurement method between two states of the same biomolecule. The method of the present invention can draw a reliable result without distortion due to multiple local energy walls different from the common structural methods by applying an energy method and can calculate the protein folding free energy efficiently. The present invention can be useful in explaining the combinational thermodynamics of protein folding and protein ligand, predicting the stability thereof, and establishing a biological treatment strategy. |
| isCitedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-106682452-A http://rdf.ncbi.nlm.nih.gov/pubchem/patent/KR-20200023940-A |
| priorityDate | 2015-04-29-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 21.