Protein elasticity determined by pressure tuning of the tyrosine residue of ubiquitin

We determined the isotropic, isothermal compressibility of ubiquitin by pressure tuning spectral holes burnt into the red edge of the absorption spectrum of the single tyrosine residue. The pressure shift is perfectly linear with burn frequency. From these data, a compressibility of 0.086 GPa(-1) in...

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Veröffentlicht in:	The Journal of chemical physics 2007-09, Vol.127 (9), p.095102-095102
Hauptverfasser:	Somoza, Mark M, Wiedersich, Johannes, Friedrich, Josef
Format:	Artikel
Sprache:	eng
Schlagworte:	Computer Simulation Elasticity Models, Chemical Models, Molecular Pressure Protein Conformation Stress, Mechanical Tyrosine - chemistry Ubiquitin - chemistry Ubiquitin - ultrastructure
Online-Zugang:	Volltext
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