期刊
JOURNAL OF MOLECULAR MODELING
卷 23, 期 7, 页码 -出版社
SPRINGER
DOI: 10.1007/s00894-017-3367-z
关键词
Protein folding; Hydrophobicity; Hydrophobic core
类别
资金
- Jagiellonian University Medical College [K/ZDS/006363]
- KNOW system
The hydrophobic core, when subjected to analysis based on the fuzzy oil drop model, appears to be a universal structural component of proteins irrespective of their secondary, supersecondary, and tertiary conformations. A study has been performed on a set of nonhomologous proteins representing a variety of CATH categories. The presence of a well-ordered hydrophobic core has been confirmed in each case, regardless of the protein's biological function, chain length or source organism. In light of fuzzy oil drop (FOD) analysis, various supersecondary forms seem to share a common structural factor in the form of a hydrophobic core, emerging either as part of the whole protein or a specific domain. The variable status of individual folds with respect to the FOD model reflects their propensity for conformational changes, frequently associated with biological function. Such flexibility is expressed as variable stability of the hydrophobic core, along with specific encoding of potential conformational changes which depend on the properties of helices and afolds.
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