کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5435184 1509149 2017 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Impact of macromolecular crowding on structure and properties of pepsin and trypsin
ترجمه فارسی عنوان
تاثیر تراکم ماکرو مولکولی بر ساختار و خواص پپسین و تریپسین
کلمات کلیدی
پراکندگی نور پویا، پراکندگی نور زاویه ای استاتیک، جمعیت انبوه، اثر حجم منحصربفرد، اثر پیری، دینامیک شیمیایی،
موضوعات مرتبط
مهندسی و علوم پایه مهندسی مواد بیومتریال
چکیده انگلیسی


- Effect of large macromolecular crowding on the structure of pepsin and trypsin
- Unfolded proteins in presence of crowding agent
- Effect of aging on the structure of the crowding agent/enzyme mixture

The change of conformation of pepsin and trypsin in absence and presence of a high molecular crowding agent has been characterized using dynamic light scattering (DLS). Structural properties were investigated as a function of chemical denaturant concentrations, the guanidine hydrochloride (GdmCl). The results showed that Ficoll 400, macromolecular crowding, has a strong effect on the chemical denaturation process of these two proteins. The changes of measured hydrodynamic radius are attributed to the enhancement effect of the crowder agent due to the excluded volume effects. The data proved that the large size of a macromolecular crowder plays a crucial role on the conformation of a protein in its unfolded states. The values of interactions Parameter kd of complex particles and a number of proteins npr attached on the Ficoll 400 measured in different GdmCl concentrations. The effect of aging on the structure of complex are studied by small angle light scattering (SALS).

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Materials Science and Engineering: C - Volume 72, 1 March 2017, Pages 98-105
نویسندگان
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