Lyophilised protein dynamics: more than just methyls?

Neutron spectroscopy has been used to probe picosecond to nanosecond dynamics in lyophilised apoferritin, insulin, superoxide dismutase and green fluorescent protein. These proteins have markedly different secondary structures yet similar CH 3 compositions. Results suggest that while only CH 3 activ...

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Veröffentlicht in:Soft matter 2012-01, Vol.8 (37), p.9529-9532
Hauptverfasser: Telling, Mark T. F, Clifton, Luke, Combet, Jérôme, Frick, Bernhard, Howells, Spencer, Sakai, Victoria García
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Sprache:eng
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Zusammenfassung:Neutron spectroscopy has been used to probe picosecond to nanosecond dynamics in lyophilised apoferritin, insulin, superoxide dismutase and green fluorescent protein. These proteins have markedly different secondary structures yet similar CH 3 compositions. Results suggest that while only CH 3 activation is apparent in apoferritin, an enhanced dynamic environment presents itself in Ins, SOD and GfP. Our results hint at a structure dependent dynamic landscape. Neutron spectroscopy has been used to probe picosecond to nanosecond dynamics in lyophilised apoferritin, insulin, superoxide dismutase and green fluorescent protein.
ISSN:1744-683X
1744-6848
DOI:10.1039/c2sm26540k