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Titolo:
Refolding of beta-lactoglobulin studied by stopped-flow circular dichroismat subzero temperatures
Autore:
Qin, ZJ; Hu, DM; Shimada, L; Nakagawa, T; Arai, M; Zhou, JM; Kihara, H;
Indirizzi:
Kansai Med Univ, Dept Phys, Hirakata, Osaka 5731136, Japan Kansai Med Univ Hirakata Osaka Japan 5731136 rakata, Osaka 5731136, Japan Acad Sinica, Inst Biophys, Natl Lab Macromol, Beijing 100101, Peoples R China Acad Sinica Beijing Peoples R China 100101 ijing 100101, Peoples R China Weifang Med Coll, Dept Diagnost, Shandong 261042, Peoples R China Weifang Med Coll Shandong Peoples R China 261042 261042, Peoples R China Unisoka Inc, Hirakata, Osaka 5730131, Japan Unisoka Inc Hirakata Osaka Japan 5730131 , Hirakata, Osaka 5730131, Japan Univ Tokyo, Sch Sci, Dept Phys, Tokyo 1130033, Japan Univ Tokyo Tokyo Japan 1130033 Sch Sci, Dept Phys, Tokyo 1130033, Japan
Titolo Testata:
FEBS LETTERS
fascicolo: 3, volume: 507, anno: 2001,
pagine: 299 - 302
SICI:
0014-5793(20011102)507:3<299:ROBSBS>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOLTEN GLOBULE; SHEET PROTEIN; ALPHA-HELIX; INTERMEDIATE; SPECTROSCOPY; ABSORPTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
19
Recensione:
Indirizzi per estratti:
Indirizzo: Kihara, H Kansai Med Univ, Dept Phys, 18-89 Uyama Higashi, Hirakata, Osaka5731136, Japan Kansai Med Univ 18-89 Uyama Higashi Hirakata Osaka Japan 5731136
Citazione:
Z.J. Qin et al., "Refolding of beta-lactoglobulin studied by stopped-flow circular dichroismat subzero temperatures", FEBS LETTER, 507(3), 2001, pp. 299-302

Abstract

Refolding of bovine beta -lactoglobulin was studied by stopped-flow circular dichroism at subzero temperatures. In ethylene glycol 45%-buffer 55% at -15 degreesC, the isomerization rate from the kinetic intermediate rich in a-helix to the native state is approximately 300-fold slower than that at 4degreesC in the absence of ethylene glycol, whereas the initial folding iscompleted within the dead time of the stopped-flow apparatus (10 ins). At -28 degreesC, we observed at least three phases; the fastest process, accompanied by an increase of alpha -helix content, is completed within the deadtime of the stopped-flow apparatus (10 ms), the second phase, accompanied by an increase of alpha -helix content with the rate of 2 s(-1), and the third phase, accompanied by a decrease of alpha -helix content. This last phase, corresponding to the isomerization process at -15 degreesC described above, was so slow that we could not monitor any changes within 4 h. Based onthe findings above, we propose that rapid alpha -helix formation and theirconcurrent collapse are common even in proteins rich in beta -structure intheir native forms. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

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Documento generato il 04/07/20 alle ore 15:03:56