Mapping electrostatic potential of a protein on its hydrophobic surface: implications for crystallization of Cytochrome P450scc.
Calculation and combined visualization of electrostatic and hydrophobic properties of Cytochrome P450scc based on two very different homology models allowed to identify extensive hydrophobic patches with neutral electrostatic potential and mutations removing such patches and thus expecting to facilitate crystallization of Cytochrome P450scc, especially for the nanotemplate crystallization method. Implications are discussed for optimizing crystallization and other aspects of protein surface properties and protein recognition.
Sivozhelezov
Victor
V
Fondazione Elba, P.zza SS. Apostoli 66, 00100 Rome, Italy.
Pechkova
Eugenia
E
Nicolini
Claudio
C
D000818:Animals; D002786:Cholesterol Side-Chain Cleavage Enzyme / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D017354:Point Mutation; D055672:Static Electricity; D013499:Surface Properties
D002786:Cholesterol Side-Chain Cleavage Enzyme