Mukesh Sharma, Ph.D.

Affiliations: 
Florida State University, Tallahassee, FL, United States 
Area:
Solid State Protein NMR
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"Mukesh Sharma"
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Timothy A. Cross grad student 2010 Florida State
 (Solution and solid state NMR spectroscopy of alpha-helical membrane proteins.)
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Publications

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Perrin BS, Tian Y, Fu R, et al. (2014) High-resolution structures and orientations of antimicrobial peptides piscidin 1 and piscidin 3 in fluid bilayers reveal tilting, kinking, and bilayer immersion. Journal of the American Chemical Society. 136: 3491-504
Perrin BS, Venable RM, Sharma M, et al. (2013) All-Atom Molecular Dynamic Simulations of Piscidin 1 and Piscidin 3 in Lipid Bilayers Biophysical Journal. 104: 600a
Miao Y, Qin H, Fu R, et al. (2012) M2 proton channel structural validation from full-length protein samples in synthetic bilayers and E. coli membranes Angewandte Chemie - International Edition. 51: 8383-8386
Dong H, Sharma M, Zhou HX, et al. (2012) Glycines: Role in α-helical membrane protein structures and a potential indicator of native conformation Biochemistry. 51: 4779-4789
Can TV, Sharma M, Hung I, et al. (2012) Magic angle spinning and oriented sample solid-state NMR structural restraints combine for influenza A M2 protein functional insights Journal of the American Chemical Society. 134: 9022-9025
Cross TA, Dong H, Sharma M, et al. (2012) M2 protein from Influenza A: From multiple structures to biophysical and functional insights Current Opinion in Virology. 2: 128-133
Hayden RM, Dao AE, Wieczorek WE, et al. (2012) The High-Resolution Structures of Two Piscidin Isoforms in Two Microbial Lipid Membrane Mimics Using Solid-State NMR Biophysical Journal. 102
Qin H, Miao Y, Fu R, et al. (2012) Structural Insights for the Full Length Influenza A M2 Proton Channel in Native E. Coli Membranes Biophysical Journal. 102: 265a
Peterson E, Ryser T, Funk S, et al. (2011) Functional reconstitution of influenza A M2(22-62) Biochimica Et Biophysica Acta - Biomembranes. 1808: 516-521
Cross TA, Sharma M, Yi M, et al. (2011) Influence of solubilizing environments on membrane protein structures Trends in Biochemical Sciences. 36: 117-125
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