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Full-Text Articles in Physical Sciences and Mathematics
Synthetic Studies In Phytochrome Chemistry, Peter A. Jacobi, Imad Odeh, Subhas Buddhu, Guolin Cai, Sundaramoorthi Rajeswari, Douglas Fry, Wanjun Zheng, Robert W. Desimone, Jiasheng Guo, Lisa D. Coutts, Sheila I. Hauck, Sam H. Leung, Indranath Ghosh, Douglas Pippin
Synthetic Studies In Phytochrome Chemistry, Peter A. Jacobi, Imad Odeh, Subhas Buddhu, Guolin Cai, Sundaramoorthi Rajeswari, Douglas Fry, Wanjun Zheng, Robert W. Desimone, Jiasheng Guo, Lisa D. Coutts, Sheila I. Hauck, Sam H. Leung, Indranath Ghosh, Douglas Pippin
Dartmouth Scholarship
An account is given of the author’s several approaches to the synthesis of the parent chromophore of phytochrome (1), a protein-bound linear tetrapyrrole derivative that controls photomorphogenesis in higher plants. These studies culminated in enantioselective syntheses of both (2R)- and (2S)-phytochromobilin (4), as well as several 13C-labeled derivatives designed to probe the site of Z,E-isomerization during photoexcitation. When reacted in vitro, synthetic 2R-4 and recombinant-derived phytochrome apoprotein N-C produced a protein-bound chromophore with identical difference spectra to naturally occurring 1.
Crystal Structure Of The Gtpase Domain Of Rat Dynamin 1, Thomas F. Reubold, Susanne Eschenburg, Andreas Becker, Marilyn Leonard, Sandra L. Schmid, Richard B. Vallee, F. Jon Kull, Dietmar J. Manstein
Crystal Structure Of The Gtpase Domain Of Rat Dynamin 1, Thomas F. Reubold, Susanne Eschenburg, Andreas Becker, Marilyn Leonard, Sandra L. Schmid, Richard B. Vallee, F. Jon Kull, Dietmar J. Manstein
Dartmouth Scholarship
Here, we present the 1.9-A crystal structure of the nucleotide-free GTPase domain of dynamin 1 from Rattus norvegicus. The structure corresponds to an extended form of the canonical GTPase fold observed in Ras proteins. Both nucleotide-binding switch motifs are well resolved, adopting conformations that closely resemble a GTP-bound state not previously observed for nucleotide-free GTPases. Two highly conserved arginines, Arg-66 and Arg-67, greatly restrict the mobility of switch I and are ideally positioned to relay information about the nucleotide state to other parts of the protein. Our results support a model in which switch I residue Arg-59 gates GTP binding …