pKD: re-designing protein pKa values | Zendy

Barbara Mary TynanConnolly | Zendy; Jens Erik Nielsen | Zendy

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pKD: re-designing protein pKa values

Author(s) -

Barbara Mary TynanConnolly,

Jens Erik Nielsen

Publication year - 2006

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/gkl192

Subject(s) - biology , mutagenesis , protein engineering , mutant , web server , enzyme , point mutation , directed evolution , protein design , computational biology , stability (learning theory) , biochemistry , microbiology and biotechnology , protein structure , computer science , gene , the internet , operating system , machine learning

The pK(a) values in proteins govern the pH-dependence of protein stability and enzymatic activity. A large number of mutagenesis experiments have been carried out in the last three decades to re-engineer the pH-activity and pH-stability profile of enzymes and proteins. We have developed the pKD webserver (http://polymerase.ucd.ie/pKa_Design), which predicts sets of point mutations that will change the pK(a) values of a set of target residues in a given direction, thus allowing for targeted re-design of the pH-dependent characteristics of proteins. The server provides the user with an interactive experience for re-designing pK(a) values by pre-calculating DeltapK(a) values from all feasible point mutations. Design solutions are found in less than 10 min for a typical design job for a medium-sized protein. Mutant DeltapK(a) values calculated by the pKD web server are in close agreement with those produced by comparing results from full-fledged pK(a) calculation methods.

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