Ontology highlight
ABSTRACT:
SUBMITTER: Kwa LG
PROVIDER: S-EPMC3988883 | biostudies-other | 2014 Apr
REPOSITORIES: biostudies-other
Journal of molecular biology 20131224 7
Three homologous spectrin domains have remarkably different folding characteristics. We have previously shown that the slow-folding R16 and R17 spectrin domains can be altered to resemble the fast folding R15, in terms of speed of folding (and unfolding), landscape roughness and folding mechanism, simply by substituting five residues in the core. Here we show that, by contrast, R15 cannot be engineered to resemble R16 and R17. It is possible to engineer a slow-folding version of R15, but our ana ...[more]