Protein Sequence- and pH-Dependent Hydration Probed by Terahertz Spectroscopy

Solvation free energy changes induced by protein folding and function are comparable to the corresponding overall free energy changes. Yet the structure, dynamics, and energetics of the protein itself have received more attention because they are easier to probe. Here we use terahertz (far-infrared)...

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Veröffentlicht in:	Journal of the American Chemical Society 2008-02, Vol.130 (8), p.2374-2375
Hauptverfasser:	Ebbinghaus, Simon, Kim, Seung Joong, Heyden, Matthias, Yu, Xin, Gruebele, Martin, Leitner, David M, Havenith, Martina
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution Hydrogen-Ion Concentration Kinetics Protein Conformation Protein Folding Protein Structure, Secondary Solvents - chemistry Spectrophotometry, Infrared - methods Surface Properties Viral Proteins - chemistry Water - chemistry
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