Dramatic Acceleration of Protein Folding by Stabilization of a Nonnative Backbone Conformation

Through a mutagenic investigation of Gly-48, a highly conserved position in the Src homology 3 domain, we have discovered a series of amino acid substitutions that are highly destabilizing, yet dramatically accelerate protein folding, some up to 10-fold compared with the wild-type rate. The unique f...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2004-05, Vol.101 (21), p.7954-7959
Hauptverfasser:	Di Nardo, Ariel A., Korzhnev, Dmitry M., Stogios, Peter J., Zarrine-Afsar, Arash, Kay, Lewis E., Davidson, Alan R., Levitt, Michael
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acid substitution Amino acids Biochemistry Biochemistry, Molecular Biology Biological Sciences Biophysics Correlations Evolution Fluorescence Glycine - genetics Glycine - metabolism Kinetics Life Sciences Magnetic Resonance Spectroscopy Mathematical functions Models, Molecular Mutation Mutation - genetics NMR Nuclear magnetic resonance Physical Sciences Protein Binding Protein Conformation Protein Denaturation Protein engineering Protein Folding Protein Renaturation Proteins - chemistry Proteins - genetics Structural Biology Thermodynamics
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!