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Myat T. Lin, Ph.D.

Affiliations: 
2010 University of Illinois, Urbana-Champaign, Urbana-Champaign, IL 
Area:
Membrane protein structure/function; Expression of membrane proteins from hyperthermophiles; Structure and mechanism of prokaryotic respiratory enzymes that generate a membrane potential
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"Myat Lin"
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Robert B. Gennis grad student 2010 UIUC
 (EPR and solid-state NMR studies on the mechanism of cytochrome BO3 ubiquinol oxidase from Escherichia coli.)

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Publications

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Iwasaki T, Miyajima-Nakano Y, Fukazawa R, et al. (2020) Escherichia coli amino acid auxotrophic expression host strains for investigating protein structure-function relationships. Journal of Biochemistry
Lin MT, Stone WD, Chaudhari V, et al. (2020) Small subunits can determine enzyme kinetics of tobacco Rubisco expressed in Escherichia coli. Nature Plants
Taguchi AT, Miyajima-Nakano Y, Fukazawa R, et al. (2017) Unpaired Electron Spin Density Distribution across Reduced [2Fe-2S] Cluster Ligands by 13Cβ-Cysteine Labeling. Inorganic Chemistry
Choi SK, Lin MT, Ouyang H, et al. (2017) Searching for the low affinity ubiquinone binding site in cytochrome bo3 from Escherichia coli. Biochimica Et Biophysica Acta
Lin MT, Fukazawa R, Miyajima-Nakano Y, et al. (2015) Escherichia coli Auxotroph Host Strains for Amino Acid-Selective Isotope Labeling of Recombinant Proteins. Methods in Enzymology. 565: 45-66
Lin MT, Occhialini A, Andralojc PJ, et al. (2015) A faster Rubisco with potential to increase photosynthesis in crops Nature. 513: 547-550
Lin MT, Fukazawa R, Miyajima-Nakano Y, et al. (2015) Escherichia coli Auxotroph Host Strains for Amino Acid-Selective Isotope Labeling of Recombinant Proteins Methods in Enzymology
Iwasaki T, Fukazawa R, Miyajima-Nakano Y, et al. (2012) Dissection of hydrogen bond interaction network around an iron-sulfur cluster by site-specific isotope labeling of hyperthermophilic archaeal Rieske-type ferredoxin. Journal of the American Chemical Society. 134: 19731-8
Lin MT, Gennis RB. (2012) Product-controlled steady-state kinetics between cytochrome aa(3) from Rhodobacter sphaeroides and equine ferrocytochrome c analyzed by a novel spectrophotometric approach. Biochimica Et Biophysica Acta. 1817: 1894-900
Lin MT, Baldansuren A, Hart R, et al. (2012) Interactions of intermediate semiquinone with surrounding protein residues at the Q(H) site of wild-type and D75H mutant cytochrome bo3 from Escherichia coli. Biochemistry. 51: 3827-38
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