http://rdf.ncbi.nlm.nih.gov/pubchem/patent/KR-20040062455-A
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_a251ae79dd7a008d95010b238c6aa1f8 http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_fdc62613fa5e5979a0cafac4a51a6ae8 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N33-6803 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-68 |
| filingDate | 2004-04-14-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_73cc6d24bbf9356a86a181cc9f426900 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_cc07fc37ba97cb90f18d0a30057a8a8c http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_e5d9cf4cfe02f19c4fa5a464dadf5255 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_41ed2e302f20a477f57da061781d7620 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_23d7592c151306f58785bc33cd00aa30 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_87b652ebb00a5e03bf0c295d95748dae http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_1f7c83c726b20b024d56926dff1f3e72 |
| publicationDate | 2004-07-07-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | KR-20040062455-A |
| titleOfInvention | Analysis of protein structure stability by thermodynamic energy functions containing high-dimensional structure of proteins |
| abstract | The present invention relates to a method for analyzing protein structure stability, and includes three secondary structures (α-helix, β-strand and loop structure), which are environmental variables, and values of the ratio exposed to the solvent depending on the degree of hydrophobicity (or solvation). 3 scores (values less than 10%, values from 10 to 50%, and more than 50%) and / or environmental scores taking into account pairwise contact of amino acids and amino acids, giving a score when the sequence is in its natural structure The score parameter is obtained by using a condition such that is always lower than the score when the competitor is in a competitive structure, and the score parameter is used to analyze whether the structure of another test protein is close to the natural structure. In other words, the method of structural stability analysis of protein by thermodynamic energy function including protein higher order structure that designs / constructs protein score (energy) function that can stabilize the natural structure of proteins through neural network learning theory and protein threading. do. Accordingly, the environmental score function considering environmental variables is introduced, and at the same time, it is useful for structural stability analysis of proteins to determine whether a given protein structure is natural by neural network learning theory and threading test. |
| priorityDate | 2004-04-14-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 427.