|
|
Avicenna Journal of Medical Biotechnology، جلد ۴، شماره ۱، صفحات ۲۳-۳۴
|
|
|
| عنوان فارسی |
|
|
| چکیده فارسی مقاله |
|
|
| کلیدواژه‌های فارسی مقاله |
|
|
| عنوان انگلیسی |
In silico Evaluation of Crosslinking Effects on Denaturant meq values and ΔCp upon Protein Unfolding |
|
| چکیده انگلیسی مقاله |
Important thermodynamic parameters including denaturant equilibrium m values (meq) and heat capacity changes (ΔCp) can be predicted based on changes in Solvent Accessible Surface Area (SASA) upon unfolding. Crosslinks such as disulfide bonds influence the stability of the proteins by decreasing the entropy gain as well as reduction of SASA of unfolded state. The aim of the study was to develop mathematical models to predict the effect of crosslinks on ΔSASA and ultimately on meq and ΔCp based on in silico methods. Changes of SASA upon computationally simulated unfolding were calculated for a set of 45 proteins with known meq and ΔCp values and the effect of crosslinks on ΔSASA of unfolding was investigated. The results were used to predict the meq of denaturation for guanidine hydrochloride and urea, as well as ΔCp for the studied proteins with overall error of 20%, 31% and 17%, re-spectively. The results of the current study were in close agreement with those obtained from the previous studies. |
|
| کلیدواژه‌های انگلیسی مقاله |
Crosslinks, Disulfides, Protein stability, Thermodynamics |
|
| نویسندگان مقاله |
|
|
| نشانی اینترنتی |
http://www.ajmb.org/En/Article.aspx?id=78 |
| فایل مقاله |
اشکال در دسترسی به فایل - ./files/site1/rds_journals/133/article-133-376185.pdf |
| کد مقاله (doi) |
|
| زبان مقاله منتشر شده |
en |
| موضوعات مقاله منتشر شده |
|
| نوع مقاله منتشر شده |
|
|
|
|
برگشت به:
صفحه اول پایگاه |
نسخه مرتبط |
نشریه مرتبط |
فهرست نشریات
|