caa a22 4500 397555628 CHVBK 20180308164801.0 cr unu---uuuuu 161202e199612 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021544 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021544 The Structure, Stability, and Folding Process of Amyloidogenic Mutant Human Lysozyme [Elektronische Daten] [Jun Funahashi, Kazufumi Takano, Kyoko Ogasahara, Yoriko Yamagata, Katsuhide Yutani] The physicochemical properties of an amyloldogenic mutant human lysozyrne (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 poiar 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. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence amyloid formation nationallicence denatured state of a protein nationallicence human lysozyme nationallicence mutant protein nationallicence stability of amyloidogenic protein nationallicence Funahashi Jun Institute for Protein Research, Osaka University 3-2 Yamadaoka, Suita, Osaka 565 aut Takano Kazufumi Institute for Protein Research, Osaka University 3-2 Yamadaoka, Suita, Osaka 565 aut Ogasahara Kyoko Institute for Protein Research, Osaka University 3-2 Yamadaoka, Suita, Osaka 565 aut Yamagata Yoriko Faculty of Pharmaceutical Sciences, Osaka University 1-6 Yamadaoka, Suita, Osaka 565 aut Yutani Katsuhide Institute for Protein Research, Osaka University 3-2 Yamadaoka, Suita, Osaka 565 aut The Journal of Biochemistry Oxford University Press 120/6(1996-12), 1216-1223 0021-924X 120:6<1216 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021544 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021544 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Funahashi Jun Institute for Protein Research, Osaka University 3-2 Yamadaoka, Suita, Osaka 565 aut NATIONALLICENCE 700 1- Takano Kazufumi Institute for Protein Research, Osaka University 3-2 Yamadaoka, Suita, Osaka 565 aut NATIONALLICENCE 700 1- Ogasahara Kyoko Institute for Protein Research, Osaka University 3-2 Yamadaoka, Suita, Osaka 565 aut NATIONALLICENCE 700 1- Yamagata Yoriko Faculty of Pharmaceutical Sciences, Osaka University 1-6 Yamadaoka, Suita, Osaka 565 aut NATIONALLICENCE 700 1- Yutani Katsuhide Institute for Protein Research, Osaka University 3-2 Yamadaoka, Suita, Osaka 565 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/6(1996-12), 1216-1223 0021-924X 120:6<1216 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford