Conformational Flexibility in a Staphylococcal Nuclease Mutant K45C from Time-Resolved Resonance Energy Transfer Measurements

Thermal fluctuations exist in native proteins and other macromolecules in solution. Some may play a role in ligand or receptor binding, control rates of enzymatic catalysis, or define a range of conformations a segment can adopt in solution. We apply the method of time-resolved resonance energy tran...

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Veröffentlicht in:	Biochemistry (Easton) 1994-08, Vol.33 (34), p.10457-10462
Hauptverfasser:	Wu, Pengguang, Brand, Ludwig
Format:	Artikel
Sprache:	eng
Schlagworte:	Energy Transfer Enzyme Stability Guanidine Guanidines Micrococcal Nuclease - chemistry Micrococcal Nuclease - genetics Molecular Structure Mutagenesis, Site-Directed Protein Conformation Protein Denaturation Solutions Spectrometry, Fluorescence Temperature Thermodynamics
Online-Zugang:	Volltext
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