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- W1987647309 abstract "In the N-terminal region of the α-helix of the c-type lysozymes, two Asx residues exist at the 18th and 27th positions. Hen lysozyme has Asp18/Asn27 (18D/27N), and we prepared three mutant lysozymes, Asn18/Asn27 (18N/27N), Asn18/Asp27 (18N/27D), and Asp18/Asp27 (18D/27D). The stability of the wild-type (18D/27N) lysozyme supported the existence of a hydrogen bond between the side chain of Asp18 and the amide group at the N1 position in the α-helix, while the stability of the 18N/27D lysozyme supported the presence of the capping box between the Ser24 (N-cap) and Asp27 residues. Although electrostatic repulsion was observed between Asp18 and Asp27 residues in 18D/27D lysozyme, the dissociation of each residue contributed to stabilizing the B-helix in 18D/27D lysozyme through hydrogen bonding and charge-helix macrodipole interaction. This is the first evidence that two neighboring negative charges at the N-terminus of the helix both increased the stability of the protein." @default.
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- W1987647309 date "1997-06-01" @default.
- W1987647309 modified "2023-09-29" @default.
- W1987647309 title "Analysis of the Stabilization of Hen Lysozyme by Helix Macrodipole and Charged Side Chain Interaction" @default.
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- W1987647309 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a021697" @default.
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