کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10537921 | 962882 | 2005 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
G148-GA3: A streptococcal virulence module with atypical thermodynamics of folding optimally binds human serum albumin at physiological temperatures
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The third albumin binding domain of streptococcal protein G strain 148 (G148-GA3) belongs to a novel class of prokaryotic albumin binding modules that is thought to support virulence in several bacterial species. Here, we characterize G148-GA3 folding and albumin binding by using differential scanning calorimetry and isothermal titration calorimetry to obtain the most complete set of thermodynamic state functions for any member of this medically significant module. When buffered at pH 7.0 the 46-amino acid alpha-helical domain melts at 72 °C and exhibits marginal stability (15 kJ/mol) at 37 °C. G148-GA3 unfolding is characterized by small contributions to entropy from non-hydrophobic forces and a low ÎCp (1.1 kJ/(deg mol)). Isothermal titration calorimetry reveals that the domain has evolved to optimally bind human serum albumin near 37 °C with a binding constant of 1.4 Ã 10 7 Mâ1. Analysis of G148-GA3 thermodynamics suggests that the domain experiences atypically small per residue changes in structural dynamics and heat capacity while transiting between folded and unfolded states.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1753, Issue 2, 1 December 2005, Pages 226-233
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1753, Issue 2, 1 December 2005, Pages 226-233
نویسندگان
David A. Rozak, John Orban, Philip N. Bryan,