期刊
BIOINFORMATION
卷 1, 期 4, 页码 127-129出版社
BIOMEDICAL INFORMATICS
DOI: 10.6026/97320630001127
关键词
hydrophobicity; active site; function recognition; protein structure
资金
- Polish State Committee for Scientific Research (KBN) [3 T11F 003 28]
- Collegium Medicum grants [501/P/133/L, WL/222/P/L.]
Recognition of a ligation site in a protein molecule is important for identifying its biological activity. The model for in silico recognition of ligation sites in proteins is presented. The idealized hydrophobic core stabilizing protein structure is represented by a three-dimensional Gaussian function. The experimentally observed distribution of hydrophobicity compared with the theoretical distribution reveals differences. The area of high differences indicates the ligation site.
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