Journal
BIOCHEMISTRY
Volume 52, Issue 29, Pages 4962-4970Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi400272q
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Funding
- National Center of Competence in Research (NCCR) in Structural Biology
- Swiss National Science Foundation [200020-137827]
- European Research Council [228076]
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Enveloping distribution sampling was used to calculate free-enthalpy changes associated with single amino acid mutations for a pair of proteins, G(A)95 and G(B)95, that show 95% sequence identity yet fold into topologically different structures. Of the L -> A, I -> F, and L -> Y mutations at positions 20, 30, and 45, respectively, of the 56-residue sequence, the first and the last contribute the most to the free-enthalpy difference between the native and non-native sequence-structure combinations, in agreement with the experimental findings for this protein pair. The individual free-enthalpy changes are almost sequence-independent in the four-strand/one-helix structure, the stable form of G(B)95, while in the three-helix bundle structure, the stable form of G(A)95, an interplay between residues 20 and 45 is observed.
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