Abstract
The conserved hydrophobic core is an important feature of a family of protein domains. We suggest a procedure for finding and the analysis of conserved hydrophobic cores. The procedure is based on using an original program called CluD (http://monkey.belozersky.msu.ru/CluD/cgi-bin/hftri.pl). Conserved hydrophobic cores of several families including homeodomains and interlock-containing domains are described. Hydrophobic clusters on some protein-DNA and protein-protein interfaces were also analyzed.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Binding Sites
-
Cluster Analysis
-
Conserved Sequence
-
DNA / chemistry*
-
DNA-Binding Proteins / chemistry*
-
Homeodomain Proteins / chemistry*
-
Hydrophobic and Hydrophilic Interactions
-
Macromolecular Substances / chemistry
-
Models, Chemical*
-
Models, Molecular*
-
Pattern Recognition, Automated / methods
-
Protein Binding
-
Sequence Alignment / methods*
-
Sequence Analysis, Protein / methods*
-
Sequence Homology, Amino Acid
Substances
-
DNA-Binding Proteins
-
Homeodomain Proteins
-
Macromolecular Substances
-
DNA