Extremophiles: Difference between revisions
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Proteins of thermophiles and halophiles tend to be more stable, and easier to manage in the laboratory, than proteins from mesophiles. Extremophile proteins have been very useful in crystallography and [[Structural genomics|structural genomics]], yielding many new structures<ref>PMID: 17563834</ref>. For example, the [[Nobel_Prizes_for_3D_Molecular_Structure|Nobel Prize-winning]] structures of the [[Ribosome|ribosome]] were determined using proteins from the thermophile ''Thermus thermophilus'' and the halophile ''Thermus thermophilus'' (see 2009 at [[Nobel Prizes for 3D Molecular Structure]]). | Proteins of thermophiles and halophiles tend to be more stable, and easier to manage in the laboratory, than proteins from mesophiles. Extremophile proteins have been very useful in crystallography and [[Structural genomics|structural genomics]], yielding many new structures<ref>PMID: 17563834</ref>. For example, the [[Nobel_Prizes_for_3D_Molecular_Structure|Nobel Prize-winning]] structures of the [[Ribosome|ribosome]] were determined using proteins from the thermophile ''Thermus thermophilus'' and the halophile ''Thermus thermophilus'' (see 2009 at [[Nobel Prizes for 3D Molecular Structure]]). | ||
==See Also (in Proteopedia)== | |||
==External Resources== | ==External Resources== | ||
*[http://en.wikipedia.org/wiki/Extremophiles Extremophiles] at Wikipedia. | *[http://en.wikipedia.org/wiki/Extremophiles Extremophiles] at Wikipedia. | ||
==References== | |||
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