Experimental pK a Value Determination of All Ionizable Groups of a Hyperstable Protein

Electrostatic interactions significantly contribute to the stability and function of proteins. The stabilizing or destabilizing effect of local charge is reflected in the perturbation of the pK value of an ionizable group from the intrinsic pK value. Herein, the charge network of a hyperstable dimer...

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Veröffentlicht in:	Chembiochem : a European journal of chemical biology 2019-04, Vol.20 (7), p.922-930
Hauptverfasser:	Raum, Heiner N, Weininger, Ulrich
Format:	Artikel
Sprache:	eng
Schlagworte:	Archaeal Proteins - chemistry Hydrogen-Ion Concentration Hydrophobic and Hydrophilic Interactions Nuclear Magnetic Resonance, Biomolecular Protein Conformation, alpha-Helical Static Electricity Sulfolobus - chemistry Thermodynamics
Online-Zugang:	Volltext
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