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Stabilization of Protein by Replacement of a Fluctuating Loop: Structural Analysis of a Chimera of Bovine α-Lactalbumin and Equine Lysozyme †

✍ Scribed by Tada, Masahito; Kobashigawa, Yoshihiro; Mizuguchi, Mineyuki; Miura, Kazunori; Kouno, Takahide; Kumaki, Yasuhiro; Demura, Makoto; Nitta, Katsutoshi; Kawano, Keiichi

Book ID
126323742
Publisher
American Chemical Society
Year
2002
Tongue
English
Weight
136 KB
Volume
41
Category
Article
ISSN
0006-2960

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Vibrational Raman optical activity (ROA) spectra of the calcium-binding lysozyme from equine milk in native and nonnative states are measured and compared with those of the homologous proteins hen egg white lysozyme and bovine ␣-lactalbumin. The ROA spectrum of holo equine lysozyme at pH 4.6 and 22°