The structure, stability, and folding process of amyloidogenic mutant human lysozyme.

The structure, stability, and folding process of amyloidogenic mutant human lysozyme. Research Abstract Details 

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The structure, stability, and folding process of amyloidogenic mutant human lysozyme. Abstract Text:

J Funahashi,K Takano,K Ogasahara,Y Yamagata,K Yutani,

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.

The structure, stability, and folding process of amyloidogenic mutant human lysozyme. Publishing Authors By Initials

J Funahashi,K Takano,K Ogasahara,Y Yamagata,K Yutani,

For similar natural sciences: physics: thermodynamics research abstracts see: natural sciences: physics: thermodynamics research

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The structure, stability, and folding process of amyloidogenic mutant human lysozyme. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 120

Page Numbers: 1216-23

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Dec

YEAR: 1996

The structure, stability, and folding process of amyloidogenic mutant human lysozyme. Information

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LANGUAGE: eng

NlmUniqueID: 376600

The structure, stability, and folding process of amyloidogenic mutant human lysozyme. Keywords Mesh Terms:

KEYWORDS: Thermodynamics

MESH TERMS: genetics

Chemical & Substance for Abstract: The structure, stability, and folding process of amyloidogenic mutant human lysozyme. Information

Substance Name: Muramidase

Registry Number: EC 3.2.1.17

Grant and Affiliation Information for The structure, stability, and folding process of amyloidogenic mutant human lysozyme.

AFFILIATION: Institute for Protein Research, Osaka University.

Country: JAPAN

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MEDLINETA: J Biochem

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