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Scientists develop protein-sequence analysis tool

entify protein active sites, and have also used this knowledge to alter enzyme functions by switching particular amino acid residues from one class of enzyme to turn it into the related but functionally different class. But comparing sequences "manually" is labor intensive, error prone, and has become impractical for those who wish to take advantage of the increasing number of sequences in protein databases, Shanklin said.

"Yet this growing data resource contains a wealth of information for structure-function studies and for protein engineering," Shanklin said. "We developed CPDL as a general tool for extracting and displaying relevant functional information from such data sets."

Also, since CPDL does not require that a protein's structure be known -- just its amino acid sequence -- it can be applied to studies of proteins that reside in the cell membrane, for which it is notoriously difficult to determine a molecular structure.


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Source:DOE/Brookhaven National Laboratory


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