@unpublished{pittir16737,
           month = {January},
           title = {CYSTEINE AND SPIN LABEL MODIFICATION AS A MEANS TO EXPLORE PROTEIN DYNAMICS AND STRUCTURE},
          author = {Marshall McGoff},
            year = {2013},
        keywords = {ESR, MSH, GB1},
             url = {http://d-scholarship-dev.library.pitt.edu/16737/},
        abstract = {The goal of this work is to expand upon the current labeling technology available in the field of site directed spin labeling (SDSL) by cysteine and spin label modification. Multiple mutants of the B1 immunoglobulin-binding domain of protein G (GB1) were expressed, purified, characterized, and described herein. The synthesis and full characterization is described for several initial compounds along the pathway to a more rigid linker with less orientational freedom. The modification of cysteine using O-mesitylenesulfonylhydroxylamine (MSH) to form dehydroalanine with subsequent attachment of a thiol is detailed in this work. Electron Spin Resonance (ESR) spectra were collected as a means for comparison to newly designed labels. Future directions for the project include the completion of the synthesis and incorporation of new spin labels using dehydroalanine.}
}