Michael Smith (kimiawan)

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Michael Smith

Dr. Michael Smith CC OBC (26 April 1932 - 4 Oktober 2000) inggih punika salah satunggaling biokimiawan pamenang Hadhiah Nobel bidang Kimia Kanada ingkang miyos wonten ing Britania Raya. [1]

Michael Smith miyos saking kulawarga pekerja wonten ing Blackpool, Inggris. Piyambakipun pikantuk gelar PhD nalika taun 1956 saking Universitas Manchester lan nglajengaken studi pascadoktoral wonten ing Laboratorium Gobind Khorana, Vancouver, Kanada. Har Gobind Khorana piyambak pikantuk Penghargaan Nobel bidang Fisiologi utawa Kedokteran nalika taun 1968 kanggé karya wonten ing kode genetik. Smith lajeng pindhah kaliyan kelompok Khorana dhateng Wisconsin, Amerika Serikat nalika taun 1960, ananging rikala taun 1961 piyambakipun wangsul malih dhateng Vancouver. sadangunipun pinten-pinten taun, Smith makarya wonten ing Fisheries Research Board of Canada Laboratory ing daerah Vancouver, lan wonten ing taun 1966 piyambakipun dipunangkat minangka profesor biokimia wonten ing Fakultas Kedokteran University of British Columbia. Michael Smith ngremeni karier riset ingkang dawa lan produktif wonten ing Universitas British Columbia. Kejawi dados profesor biokimia lan investigator karier MRC, Smith ugi minangka direktur pendiri Biotechnology Laboratory saking taun 1987 dumugi ing taun 1995. Dr. Smith ugi minangka pimpinan ilmiah ingkang angka pisanan wonten ing Protein Engineering Network Centers of Excellence. Nalika taun 1996 Smith dipunangkat minangka Profesor Istimewa Bioteknologi Peter Wall lan salajengipun direktur pendiri Genome Sequencing Center wonten ing BC Cancer Research Agency. [2]

Wonten ing taun 1993, Dr. Michael Smith pikantuk Penghargaan Nobel sesarengan kaliyan Kary Mullis kanggé pengembangan teknik mutagenesis ingkang dipunarahaken dhateng sasaran, teknik ingkang mungkinaken sekuens DNA saking saben gen dipunéwahi kanthi cara dipuntunjuk. Michael Smith nyumbangaken sepalih artanipun saking Hadhiah Nobel wonten ing para panliti ingkang makarya babagan genetika skizofrenia. Sepalih ingkang sanésipun dipunparingaken dhateng Science World BC lan Society for Canadian Women in Science and Technology. Royal Bank Award, ingkang dipuntampi Michael Smith nalika taun 1999, kalebet ugi dana rekan ingkang langsung dipunsumbangaken dhateng BC Cancer Foundation.[3]

Karya pilihan[sunting | sunting sumber]

  • Ferrer, J.C., Turano, P., Banci, L., Bertini, I., Morris, I.K., Smith, K.M., Smith, M., Mauk, A.G. (1994). Active site coordination chemistry of the cytochrome c peroxidase Asp235Ala variant: Spectroscopic and functional characterization. Biochem. 33: (25) 7819-7829.
  • Guillemette, J.G., Barker, P.D., Eltis, L.D., Lo, T.P., Smith, M., Brayer, G.D., Mauk, A.G. (1994). Analysis of the biomolecular reducation of ferricytochrome c by ferrocytochrome b5 through mutagenesis and molecular modelling. Biochimie 76: 592-604.
  • Berghuis, A.M., Guillemette, J.G., Smith, M., and Brayer, G.D. (1994). Mutation of tyrosine-67 to phenylamaine in cytochrome c significantly alters the local heme environment. J. Mol. Biol. 235: 1326-1341.
  • Rafferty, S.P., Guillemette, J.G., Smith, M., and Mauk, A.G. (1996). Azide binding and active site dynamics of position-82 variants of ferricytochrome c. Inorg. Chem. Acta.242: 171-177.
  • Woods, A.C., Guillemette, J.G., Parraish, J.C., Smith, M., Wallace, C.J.A. (1996). Synergy in Protein Engineering. Mutagenic manipulation of protein structure to simplify semisynthesis. J. Biol. Chem. 271: (50) 32008-32015.
  • Hildebrand, D.P., Ferrer, J.C., Tang, H.-L., Smith, M., and Mauk, A.G. (1996). Trans effects on cysteine ligation in the proximal His93Cys variant of horse heart myoglobin. Biochemistry 34: 11598-11605.
  • Hildebrand, D.P., Ferrer, J.C., Tang, H.-L., Luo, Y., Hunter, C.L., Brayer, G.D., Smith, M. and Mauk, A.G. (1996). Efficient coupled oxidation of heme by an active site variant of horse heart myoglobin. J. Am. Chem. Soc. 118: (51) 12909-12915.
  • Manurus, R., Overall, C.M., Bogumil, R., Luo, Y., Mauk, A.G., Smith, M., and Brayer, G.D. (1997). Thermal stabilization of horse heart myoglobin through modification of ahydrophobic cluster in the proximal heme pocket. Biochem. Acta. 1341: 1-13.[4]

Cathetan Suku[sunting | sunting sumber]

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