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• W2067244262 startingPage "271" @default.
• W2067244262 abstract "The usefulness of molecular dynamics to assess the structural integrity of mutants containing several mutations has been investigated. Our goal was to determine whether molecular dynamics would be able to discriminate mutants of a protein having a close-to-wild-type fold, from those that are not folded under the same conditions. We used as a model the B1 domain of protein G in which we replaced the unique central alpha-helix by the sequence of the second beta-hairpin, which has a strong intrinsic propensity to form this secondary structure in solution. In the resulting protein, one-third of the secondary structure has been replaced by a non-native one. Models of the mutants were built based on the three-dimensional structure of the wild-type GB1 domain. During 2 ns of molecular dynamics simulations on these models, mutants containing up to 10 mutations in the helix retained the native fold, while another mutant with an additional mutation unfolded. This result is in agreement with our circular dichroism and NMR experiments, which indicated that the former mutants fold into a structure similar to the wild-type, as opposed to the latter mutant which is partly unfolded. Additionally, a mutant containing six mutations scattered through the surface of the domain, and which is unfolded, was also detected by the simulation. This study suggests that molecular dynamics calculations could be performed on molecular models of mutants of a protein to evaluate their foldability, prior to a mutagenesis experiment." @default.
• W2067244262 created "2016-06-24" @default.
• W2067244262 creator A5037478983 @default.
• W2067244262 creator A5080707475 @default.
• W2067244262 date "2008-12-31" @default.
• W2067244262 modified "2023-10-09" @default.
• W2067244262 title "Molecular dynamics as a tool to detect protein foldability. A mutant of domain B1 of protein G with non-native secondary structure propensities" @default.
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• W2067244262 doi "https://doi.org/10.1110/ps.8.2.271" @default.
• W2067244262 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2144254" @default.
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