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رابطه بین فعالیت Rnase A با فاصله بین Nε2-His12 وNδ1- His119 تحت اثر افزایش نمکهای پایدار کننده و ناپایدار کننده

موسوی موحدی, علی اکبر ، قرنفولی, محسن ، جلیلی, سیف اله ، احمد, فیضان ، چمنی, جمشید خان ، حکیم الهی, غلامحسین ، صادقی, مهدی ، امانی, مجتبی ، صبوری, علی اکبر (1384) رابطه بین فعالیت Rnase A با فاصله بین Nε2-His12 وNδ1- His119 تحت اثر افزایش نمکهای پایدار کننده و ناپایدار کننده. The Protein Journal ــ 25 (2). ص.ص.117-125. شاپا 1572-3887

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عنوان انگليسی

The correlation of RNase A enzymatic activity with the changes in the distance between Nepsilon2-His12 and N delta1-His119 upon addition of stabilizing and destabilizing salts.

خلاصه انگلیسی

The effect of stabilizing and destabilizing salts on the catalytic behavior of ribonuclease A (RNase A) was investigated at pH 7.5 and 25 degrees C, using spectrophotometric, viscometric and molecular dynamic methods. The changes in the distance between N(epsilon2) of His(12) and N(delta1) of His(119) at the catalytic center of RNase A upon the addition of sodium sulfate, sodium hydrogen sulfate and sodium thiocyanate were evaluated by molecular dynamic methods. The compactness and expansion in terms of Stokes radius of RNase A upon the addition of sulfate ions as kosmotropic salts, and thiocyanate ion as a chaotropic salt, were estimated by viscometric measurements. Enzyme activity was measured using cytidine 2', 3'-cyclic monophosphate as a substrate. The results from the measurements of distances between N(epsilon2) of His(12) and N(delta1) of His(119) and Stokes radius suggest (i) that the presence of sulfate ions decreases the distance between the catalytic His residues and increases the globular compactness, and (ii) that there is an expansion of the enzyme surface as well as elongation of the catalytic center in the presence of thiocyanate ion. These findings are in agreement with activity measurements.

نوع سند :مقاله
زبان سند : انگلیسی
نویسنده مسئول :علی اکبر موسوی موحدی
ضریب تاثیر و نمایه مجلات:cited By (since 1996) 1
کلیدواژه ها (انگلیسی):cytidine derivative; ribonuclease A; sodium hydrogen sulfate; sodium sulfate; sulfate; thiocyanate sodium; thiocyanic acid derivative; unclassified drug, article; catalysis; enzyme activity; molecular dynamics; spectrophotometry; viscometry, Kinetics; Models, Molecular; Point Mutation; Protein Conformation; Protein Folding; Ribonuclease, Pancreatic; Salts; Temperature
موضوعات :QU بیوشیمی
بخش های دانشگاهی :دانشكده پزشكي > گروه علوم پایه > بخش بیوفیزیک
کد شناسایی :1067
ارائه شده توسط : خانم صغری گلمغانی
ارائه شده در تاریخ :13 اسفند 1388 07:12
آخرین تغییر :20 فروردین 1393 13:12

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