http://rdf.ncbi.nlm.nih.gov/pubchem/patent/KR-20040052611-A

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filingDate 2004-04-14-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_87b652ebb00a5e03bf0c295d95748dae
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publicationDate 2004-06-23-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber KR-20040052611-A
titleOfInvention Analysis of protein structure stability by statistical environment score function containing Ramachandran angle
abstract The present invention relates to a method for analyzing protein structure stability, and includes three types of secondary structure (α-helix, β-strand and loop structure), which are general environmental covariating variables, and the degree of exposure to solvent depending on the degree of hydrophobicity (or solvation). In addition to the three values of (less than 10%, 10-50%, and more than 50%), the Ramachandran angle, where each amino acid represents spatial constraints due to the influence of residues, is introduced in the statistical method. The technical point of this invention is to accurately describe the environment of amino acids constituting each protein by obtaining an environmental score function. That is, in the method of recognizing natural structure by forming decoy structure using other known protein structure data and comparing natural structure and decoy structure using the environmental score function, by considering Ramachandran angle Due to the higher reliability it can be useful for structural stability analysis of proteins.
priorityDate 2004-04-14-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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Total number of triples: 25.