Mapping transition states of protein unfolding by protein engineering of ligand-binding sites

We describe a method for probing the integrity and relative orientation of structural elements that are indirectly linked by ligands in protein complexes during protein folding. The effect of 3′-GMP on the rate constants of unfolding of wild-type barnase and several mutants has been studied. By comp...

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Veröffentlicht in:	Journal of molecular biology 1991-10, Vol.221 (3), p.1007-1014
Hauptverfasser:	Sancho, Javier, Meiering, Elizabeth M., Fersht, Alan R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Proteins barnase Binding Sites Biological and medical sciences Conformational dynamics in molecular biology engineering Escherichia coli Fundamental and applied biological sciences. Psychology Guanosine Monophosphate - chemistry Kinetics Ligands Molecular biophysics pathway protein Protein Conformation Protein Engineering Recombinant Proteins - chemistry Ribonucleases - chemistry stability Thermodynamics Urea - chemistry
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