Cargando…
Reinvestigation of the Oxidative Folding Pathways of Hen Egg White Lysozyme: Switching of the Major Pathways by Temperature Control
It has been well established that in the oxidative folding of hen egg white lysozyme (HEL), which has four SS linkages in the native state (N), three des intermediates, i.e., des[76–94], des[64–80], and des [6–127], are populated at 20 °C and N is dominantly formed by the oxidation of des[64–80] and...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Molecular Diversity Preservation International (MDPI)
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3742182/ https://www.ncbi.nlm.nih.gov/pubmed/23803654 http://dx.doi.org/10.3390/ijms140713194 |
_version_ | 1782280328035958784 |
---|---|
author | Arai, Kenta Shibagaki, Wataru Shinozaki, Reina Iwaoka, Michio |
author_facet | Arai, Kenta Shibagaki, Wataru Shinozaki, Reina Iwaoka, Michio |
author_sort | Arai, Kenta |
collection | PubMed |
description | It has been well established that in the oxidative folding of hen egg white lysozyme (HEL), which has four SS linkages in the native state (N), three des intermediates, i.e., des[76–94], des[64–80], and des [6–127], are populated at 20 °C and N is dominantly formed by the oxidation of des[64–80] and des[6–127]. To elucidate the temperature effects, the oxidative folding pathways of HEL were reinvestigated at 5–45 °C in the presence of 2 M urea at pH 8.0 by using a selenoxide reagent, DHS(ox). When reduced HEL was reacted with 1–4 equivalents of DHS(ox), 1S, 2S, 3S, and 4S intermediate ensembles with 1–4 SS linkages, respectively, were produced within 1 min. After the oxidation, 3S was slowly converted to the des intermediates with formation of the native structures through SS rearrangement. At 5 °C, des[76–94] was populated in the largest amount, but the oxidation to N was slower than that of des[64–80] and des[6–127]. At 35 °C, on the other hand, des[64–80] and des[6–127] were no longer stable, and only des[76–94] was populated. The results suggested that the major folding pathways of HEL can be switched from one to the other by temperature control. |
format | Online Article Text |
id | pubmed-3742182 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
spelling | pubmed-37421822013-08-13 Reinvestigation of the Oxidative Folding Pathways of Hen Egg White Lysozyme: Switching of the Major Pathways by Temperature Control Arai, Kenta Shibagaki, Wataru Shinozaki, Reina Iwaoka, Michio Int J Mol Sci Article It has been well established that in the oxidative folding of hen egg white lysozyme (HEL), which has four SS linkages in the native state (N), three des intermediates, i.e., des[76–94], des[64–80], and des [6–127], are populated at 20 °C and N is dominantly formed by the oxidation of des[64–80] and des[6–127]. To elucidate the temperature effects, the oxidative folding pathways of HEL were reinvestigated at 5–45 °C in the presence of 2 M urea at pH 8.0 by using a selenoxide reagent, DHS(ox). When reduced HEL was reacted with 1–4 equivalents of DHS(ox), 1S, 2S, 3S, and 4S intermediate ensembles with 1–4 SS linkages, respectively, were produced within 1 min. After the oxidation, 3S was slowly converted to the des intermediates with formation of the native structures through SS rearrangement. At 5 °C, des[76–94] was populated in the largest amount, but the oxidation to N was slower than that of des[64–80] and des[6–127]. At 35 °C, on the other hand, des[64–80] and des[6–127] were no longer stable, and only des[76–94] was populated. The results suggested that the major folding pathways of HEL can be switched from one to the other by temperature control. Molecular Diversity Preservation International (MDPI) 2013-06-26 /pmc/articles/PMC3742182/ /pubmed/23803654 http://dx.doi.org/10.3390/ijms140713194 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland http://creativecommons.org/licenses/by/3.0 This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Arai, Kenta Shibagaki, Wataru Shinozaki, Reina Iwaoka, Michio Reinvestigation of the Oxidative Folding Pathways of Hen Egg White Lysozyme: Switching of the Major Pathways by Temperature Control |
title | Reinvestigation of the Oxidative Folding Pathways of Hen Egg White Lysozyme: Switching of the Major Pathways by Temperature Control |
title_full | Reinvestigation of the Oxidative Folding Pathways of Hen Egg White Lysozyme: Switching of the Major Pathways by Temperature Control |
title_fullStr | Reinvestigation of the Oxidative Folding Pathways of Hen Egg White Lysozyme: Switching of the Major Pathways by Temperature Control |
title_full_unstemmed | Reinvestigation of the Oxidative Folding Pathways of Hen Egg White Lysozyme: Switching of the Major Pathways by Temperature Control |
title_short | Reinvestigation of the Oxidative Folding Pathways of Hen Egg White Lysozyme: Switching of the Major Pathways by Temperature Control |
title_sort | reinvestigation of the oxidative folding pathways of hen egg white lysozyme: switching of the major pathways by temperature control |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3742182/ https://www.ncbi.nlm.nih.gov/pubmed/23803654 http://dx.doi.org/10.3390/ijms140713194 |
work_keys_str_mv | AT araikenta reinvestigationoftheoxidativefoldingpathwaysofheneggwhitelysozymeswitchingofthemajorpathwaysbytemperaturecontrol AT shibagakiwataru reinvestigationoftheoxidativefoldingpathwaysofheneggwhitelysozymeswitchingofthemajorpathwaysbytemperaturecontrol AT shinozakireina reinvestigationoftheoxidativefoldingpathwaysofheneggwhitelysozymeswitchingofthemajorpathwaysbytemperaturecontrol AT iwaokamichio reinvestigationoftheoxidativefoldingpathwaysofheneggwhitelysozymeswitchingofthemajorpathwaysbytemperaturecontrol |