Investigation of an Anomalously Accelerating Substitution in the Folding of a Prototypical Two-State Protein
Abstract
The folding rates of two-state single-domain proteins are generally resistant to small-scale changes in amino acid sequence. For example, having surveyed here over 700 single-residue substitutions in 24 well-characterized two-state proteins, we find that the majority (55%) of these substitutions affect folding rates by less than a factor of 2, and that only 9% affect folding rates by more than a factor of 8. Among those substitutions that...
Paper Details
Title
Investigation of an Anomalously Accelerating Substitution in the Folding of a Prototypical Two-State Protein
Published Date
Oct 1, 2010
Journal
Volume
403
Issue
3
Pages
446 - 458
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