Martin Sagermann

Affiliations: 
Chemistry University of California, Santa Barbara, Santa Barbara, CA, United States 
Area:
Biochemistry
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"Martin Sagermann"
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Publications

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Takenoya M, Nikolakakis K, Sagermann M. (2010) Crystallographic insights into the pore structures and mechanisms of the EutL and EutM shell proteins of the ethanolamine-utilizing microcompartment of Escherichia coli. Journal of Bacteriology. 192: 6056-63
Chapleau RR, Sagermann M. (2009) Real-time in vivo imaging of mercury uptake in Caenorhabditis elegans through the foodchain. Toxicology. 261: 136-42
Sagermann M, Ohtaki A, Nikolakakis K. (2009) Crystal structure of the EutL shell protein of the ethanolamine ammonia lyase microcompartment. Proceedings of the National Academy of Sciences of the United States of America. 106: 8883-7
Nikolakakis K, Ohtaki A, Newton K, et al. (2009) Preliminary structural investigations of the Eut-L shell protein of the ethanolamine ammonia-lyase metabolosome of Escherichia coli Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 65: 128-132
Sagermann M, Chapleau RR, DeLorimier E, et al. (2009) Using affinity chromatography to engineer and characterize pH-dependent protein switches. Protein Science : a Publication of the Protein Society. 18: 217-28
Chapleau RR, Blomberg R, Ford PC, et al. (2008) Design of a highly specific and noninvasive biosensor suitable for real-time in vivo imaging of mercury (II) uptake. Protein Science : a Publication of the Protein Society. 17: 614-22
Sagermann M, Baase WA, Matthews BW. (2006) Sequential reorganization of beta-sheet topology by insertion of a single strand. Protein Science : a Publication of the Protein Society. 15: 1085-92
Sagermann M, Baase WA, Mooers BH, et al. (2004) Relocation or duplication of the helix A sequence of T4 lysozyme causes only modest changes in structure but can increase or decrease the rate of folding. Biochemistry. 43: 1296-301
Sagermann M, Gay L, Matthews BW. (2003) Long-distance conformational changes in a protein engineered by modulated sequence duplication. Proceedings of the National Academy of Sciences of the United States of America. 100: 9191-5
Sagermann M, Matthews BW. (2002) Crystal structures of a T4-lysozyme duplication-extension mutant demonstrate that the highly conserved beta-sheet region has low intrinsic folding propensity. Journal of Molecular Biology. 316: 931-40
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