Study of Growth Hormones Folding: First-order-like Phase Transition Model

碩士 === 國立中興大學 === 生物化學研究所 === 90 === The folding of a protein may be a spontaneous process and independent of its folding path but it may misfold and aggregate. Thus, we designed a stepwise quasi-static process to restore the growth hormone structures and to change refolding potentials of...

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Main Authors: Ming-Sinng Cheng, 鄭銘松
Other Authors: Lou-Sing Kan
Format: Others
Language:zh-TW
Published: 2002
Online Access:http://ndltd.ncl.edu.tw/handle/18488026039824880761
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spelling ndltd-TW-090NCHU01070292016-06-27T16:09:33Z http://ndltd.ncl.edu.tw/handle/18488026039824880761 Study of Growth Hormones Folding: First-order-like Phase Transition Model 生長激素摺疊之研究-似一階相變反應模型 Ming-Sinng Cheng 鄭銘松 碩士 國立中興大學 生物化學研究所 90 The folding of a protein may be a spontaneous process and independent of its folding path but it may misfold and aggregate. Thus, we designed a stepwise quasi-static process to restore the growth hormone structures and to change refolding potentials of the solvents in a gradual manner in the hope that conformational changes of the associated intermediates, Mi (i = 1 to n), between U and N, might be detected by circular dichroism spectroscopy (CD) and dynamic light scattering (DLS). Conformation analysis of the CD spectra of the refolding intermediates indicated that the secondary structures were restored in the initial refolding intermediate. However, the tertiary interactions within the protein were restored during the last two refolding stages, as elucidated by thermal stability tests. DLS analysis suggested that the average hydrodynamic radii of the refolding intermediates shrunk to native-like-size after the first refolding stage. Our observations suggest that stable protein refolding intermediates can be obtained by using quasi-static TED processes. Namely, an unfolded protein which refolds back through a carefully designed stepwise quasi-static-like process may experience a gradual change in its environment and thus will not be trapped in a “burst phase” or form aggregates. Lou-Sing Kan 甘魯生 2002 學位論文 ; thesis 59 zh-TW
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description 碩士 === 國立中興大學 === 生物化學研究所 === 90 === The folding of a protein may be a spontaneous process and independent of its folding path but it may misfold and aggregate. Thus, we designed a stepwise quasi-static process to restore the growth hormone structures and to change refolding potentials of the solvents in a gradual manner in the hope that conformational changes of the associated intermediates, Mi (i = 1 to n), between U and N, might be detected by circular dichroism spectroscopy (CD) and dynamic light scattering (DLS). Conformation analysis of the CD spectra of the refolding intermediates indicated that the secondary structures were restored in the initial refolding intermediate. However, the tertiary interactions within the protein were restored during the last two refolding stages, as elucidated by thermal stability tests. DLS analysis suggested that the average hydrodynamic radii of the refolding intermediates shrunk to native-like-size after the first refolding stage. Our observations suggest that stable protein refolding intermediates can be obtained by using quasi-static TED processes. Namely, an unfolded protein which refolds back through a carefully designed stepwise quasi-static-like process may experience a gradual change in its environment and thus will not be trapped in a “burst phase” or form aggregates.
author2 Lou-Sing Kan
author_facet Lou-Sing Kan
Ming-Sinng Cheng
鄭銘松
author Ming-Sinng Cheng
鄭銘松
spellingShingle Ming-Sinng Cheng
鄭銘松
Study of Growth Hormones Folding: First-order-like Phase Transition Model
author_sort Ming-Sinng Cheng
title Study of Growth Hormones Folding: First-order-like Phase Transition Model
title_short Study of Growth Hormones Folding: First-order-like Phase Transition Model
title_full Study of Growth Hormones Folding: First-order-like Phase Transition Model
title_fullStr Study of Growth Hormones Folding: First-order-like Phase Transition Model
title_full_unstemmed Study of Growth Hormones Folding: First-order-like Phase Transition Model
title_sort study of growth hormones folding: first-order-like phase transition model
publishDate 2002
url http://ndltd.ncl.edu.tw/handle/18488026039824880761
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