کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
10870321 1073998 2014 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Forces stabilizing proteins
ترجمه فارسی عنوان
نیروهای ثبات پروتئین ها
کلمات کلیدی
پایداری پروتئین، تعاملات هیدروفوبیک، پیوند های هیدروژنی، آنتروپی سازگار،
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
چکیده انگلیسی
The goal of this article is to summarize what has been learned about the major forces stabilizing proteins since the late 1980s when site-directed mutagenesis became possible. The following conclusions are derived from experimental studies of hydrophobic and hydrogen bonding variants. (1) Based on studies of 138 hydrophobic interaction variants in 11 proteins, burying a -CH2− group on folding contributes 1.1 ± 0.5 kcal/mol to protein stability. (2) The burial of non-polar side chains contributes to protein stability in two ways: first, a term that depends on the removal of the side chains from water and, more importantly, the enhanced London dispersion forces that result from the tight packing in the protein interior. (3) Based on studies of 151 hydrogen bonding variants in 15 proteins, forming a hydrogen bond on folding contributes 1.1 ± 0.8 kcal/mol to protein stability. (4) The contribution of hydrogen bonds to protein stability is strongly context dependent. (5) Hydrogen bonds by side chains and peptide groups make similar contributions to protein stability. (6) Polar group burial can make a favorable contribution to protein stability even if the polar group is not hydrogen bonded. (7) Hydrophobic interactions and hydrogen bonds both make large contributions to protein stability.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 588, Issue 14, 27 June 2014, Pages 2177-2184
نویسندگان
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