کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8292004 | 1536488 | 2008 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Electrostatic interactions in the denatured state ensemble: Their effect upon protein folding and protein stability
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کلمات کلیدی
Ribosomal protein L9Denatured state ensembleThermodynamic linkage - اتصال ترمودینامیکیProtein folding - تاشدگی پروتئینpH titration - تثبیت pHelectrostatic interactions - تعاملات الکترواستاتیکunfolded state - دولت انحصاریProtein design - طراحی پروتئینProtein engineering - مهندسی پروتئینProtein stability - پایداری پروتئین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
It is now recognized that the denatured state ensemble (DSE) of proteins can contain significant amounts of structure, particularly under native conditions. Well-studied examples include small units of hydrogen bonded secondary structure, particularly helices or turns as well as hydrophobic clusters. Other types of interactions are less well characterized and it has often been assumed that electrostatic interactions play at most a minor role in the DSE. However, recent studies have shown that both favorable and unfavorable electrostatic interactions can be formed in the DSE. These can include surprisingly specific non-native interactions that can even persist in the transition state for protein folding. DSE electrostatic interactions can be energetically significant and their modulation either by mutation or by varying solution conditions can have a major impact upon protein stability. pH dependent stability studies have shown that electrostatic interactions can contribute up to 4 kcal mol-1 to the stability of the DSE.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 469, Issue 1, 1 January 2008, Pages 20-28
Journal: Archives of Biochemistry and Biophysics - Volume 469, Issue 1, 1 January 2008, Pages 20-28
نویسندگان
Jae-Hyun Cho, Satoshi Sato, Jia-Cherng Horng, Burcu Anil, Daniel P. Raleigh,