Bruce Macher

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Determining the number and location of disulfide bonds within a protein provide valuable insight into the protein's three-dimensional structure. Purely computational methods that predict the bonded cysteine pairings given a protein's primary structure have limitations in both prediction correctness and the number of bonds that can be predicted. Our approach(More)
The tertiary structure and biological function of a protein can be better understood given knowledge of the number and location of its disulfide bonds. By utilizing mass spectrometric (MS) experimental procedures that produce spectra of the protein's peptides joined by a disulfide bond, we can make initial identifications of these bonded cysteine pairings.(More)
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