Abstract:
:This paper describes a theory for the mechanism of three-state transition of proteins which is often observed in aqueous organic cosolvent systems, i.e., from the native, via intermediate to helical forms. The first transition, accompanied by changes in the tertiary and/or secondary structures, was explained by larger bindings of the organic solvent molecules to the intermediate than to the native state; the second transition, resulting in changes mainly in the secondary structure, i.e., helical transition, was explained by less hydration sites for the helical state. Computer simulations of the transition were carried out using plausible values for the number of alcohol and water binding sites of proteins as well as for the equilibrium constant of the transitions in the absence of cosolvent. A reasonable agreement with the experimental transitions was observed. The stronger effect of alcohols with longer alkyl chains was explained by their greater binding to nonpolar groups and their larger exclusion from peptide groups.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Arakawa T,Goddette Ddoi
10.1016/0003-9861(85)90004-9subject
Has Abstractpub_date
1985-07-01 00:00:00pages
21-32issue
1eissn
0003-9861issn
1096-0384pii
0003-9861(85)90004-9journal_volume
240pub_type
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journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
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更新日期:2007-12-01 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1006/abbi.1999.1403
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更新日期:2007-08-01 00:00:00
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journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
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