Article
Stability and solvation of Thr/Ser to Ala and Gly mutations at the N-cap of alpha-helices.
FEBS letters - 27 Jun 1994
Chen Y W, Fersht A R
Abstract excerpt
The solvation of polar groups at the N-terminal end of alpha-helices was studied by comparing the crystal structures of T4 lysozyme, barley chymotrypsin inhibitor 2 (CI2), barnase and their respective N-cap mutants. Whether or not the N3 residue is solvated on mutating the N-cap Thr/Ser to Ala or Gly appears to be related to the identities and the side-chain conformations of the N2 and N3 residues. When these two...
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