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Title
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The structure, stability, and folding process of amyloidogenic mutant human lysozyme.
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Authors
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J.Funahashi,
K.Takano,
K.Ogasahara,
Y.Yamagata,
K.Yutani.
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Ref.
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J Biochem (tokyo), 1996,
120,
1216-1223.
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PubMed id
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Abstract
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The physicochemical properties of an amyloidogenic mutant human lysozyme
(Ile56Thr) were examined in order to elucidate the mechanism of amyloid
formation. The crystal structure of the mutant protein was the same as the
wild-type structure, except that the hydroxyl group of the introduced Thr56
formed a hydrogen bond with a water molecule in the interior of the protein. The
other physicochemical properties of the mutant protein in the native state were
not different from those of the wild-type protein. However, the equilibrium and
kinetic stabilities of the mutant protein were remarkably decreased due to the
introduction of a polar residue (Thr) in the interior of the molecule. It can be
concluded that the amyloid formation of the mutant human lysozyme is due to a
tendency to favor (partly or/and completely) denatured structures.
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