The Folding Trajectory of RNase H Is Dominated by Its Topology and Not Local Stability: A Protein Engineering Study of Variants that Fold via Two-State and Three-State Mechanisms

Proteins can sample a variety of partially folded conformations during the transition between the unfolded and native states. Some proteins never significantly populate these high-energy states and fold by an apparently two-state process. However, many proteins populate detectable, partially folded...

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Veröffentlicht in:	Journal of molecular biology 2009-08, Vol.391 (2), p.450-460
Hauptverfasser:	Connell, Katelyn B., Miller, Erik J., Marqusee, Susan
Format:	Artikel
Sprache:	eng
Schlagworte:	Enzyme Stability Escherichia coli Escherichia coli - enzymology intermediates Mutation Protein Conformation Protein Engineering Protein Folding Ribonuclease H - chemistry Ribonuclease H - genetics RNase H topology transition state
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