Temperature-dependent conformational change affecting Tyr11 and sweetness loops of brazzein

The sweet protein brazzein, a member of the Csβα fold family, contains four disulfide bonds that lend a high degree of thermal and pH stability to its structure. Nevertheless, a variable temperature study has revealed that the protein undergoes a local, reversible conformational change between 37 an...

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Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2013-06, Vol.81 (6), p.919-925
Hauptverfasser:	Cornilescu, Claudia C., Cornilescu, Gabriel, Rao, Hongyu, Porter, Sarah F., Tonelli, Marco, DeRider, Michele L., Markley, John L., Assadi-Porter, Fariba M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Brassicaceae - chemistry human sweet receptor Humans Models, Molecular NMR spectroscopy Nuclear Magnetic Resonance, Biomolecular Plant Proteins - chemistry Protein Conformation Receptors, G-Protein-Coupled - chemistry Receptors, G-Protein-Coupled - genetics Receptors, G-Protein-Coupled - metabolism saturation transfer difference spectroscopy sweet protein Sweetening Agents - chemistry three-dimensional solution structures
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