Mobility and structure of human serum albumin powders in water-acetonitrile mixtures by1H NMR relaxation and FTIR spectroscopy

The effect of acetonitrile on protein dynamics was investigated for solid human serum albumin samples at various hydration levels. Temperature dependences of1H nonselective nuclear magnetic resonanceT1 andT2 relaxation times at 27 MHz have been measured and data were interpreted in terms of three ki...

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Veröffentlicht in:	Applied magnetic resonance 2005-09, Vol.29 (3), p.421-437
Hauptverfasser:	Belskaya, A. V., Fayzullin, D. A., Fedotov, V. D.
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetonitrile Magnetic induction NMR Nuclear magnetic resonance Proteins Serum albumin
Online-Zugang:	Volltext
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