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翻訳と辞書　辞書検索 [ 開発暫定版 ] スポンサード リンク Equilibrium unfolding ： ウィキペディア英語版 Equilibrium unfolding In biochemistry, equilibrium unfolding is the process of unfolding a protein or RNA molecule by gradually changing its environment, such as by changing the temperature or pressure, adding chemical denaturants, or applying force as with an atomic force microscope tip. Since equilibrium is maintained at all steps, the process is reversible (equilibrium folding). Equilibrium unfolding is used to determine the conformational stability of the molecule. ==Theoretical background== In its simplest form, equilibrium unfolding assumes that the molecule may belong to only two thermodynamic states, the ''folded state'' (typically denoted ''N'' for "native" state) and the unfolded state (typically denoted ''U''). This "all-or-none" model of protein folding was first proposed by Tim Anson in 1945,〔Anson ML, Protein Denaturation and the Properties of Protein Groups, Advances in Protein Chemistry, 2, 361-386 (1945)〕 but is believed to hold only for small, single structural domains of proteins (Jackson, 1998); larger domains and multi-domain proteins often exhibit intermediate states. As usual in statistical mechanics, these states correspond to ensembles of molecular conformations, not just one conformation. The molecule may transition between the native and unfolded states according to a simple kinetic model :N U with rate constants $k\_$ and $k\_$ for the folding ($U\; \backslash rightarrow\; N$) and unfolding ($N\; \backslash rightarrow\; U$) reactions, respectively. The dimensionless equilibrium constant $K\_\; \backslash \; \backslash stackrel\backslash \; \backslash frac\}\; =\; \backslash frac\}$ can be used to determine the conformational stability $\backslash Delta\; G^o$ by the equation :$$ \Delta G^ o = -RT \ln K_ where $R$ is the gas constant and $T$ is the absolute temperature in kelvins. Thus, $\backslash Delta\; G^o$ is positive if the unfolded state is less stable (i.e., disfavored) relative to the native state. The most direct way to measure the conformational stability $\backslash Delta\; G^o$ of a molecule with two-state folding is to measure its kinetic rate constants $k\_$ and $k\_$ under the solution conditions of interest. However, since protein folding is typically completed in milliseconds, such measurements can be difficult to perform, usually requiring expensive stopped flow or (more recently) continuous-flow mixers to provoke folding with a high time resolution. Dual polarisation interferometry is an emerging technique to directly measure conformational change and $\backslash Delta\; G^o$. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Equilibrium unfolding」の詳細全文を読む スポンサード リンク 翻訳と辞書 : 翻訳のためのインターネットリソース Copyright(C) kotoba.ne.jp 1997-2016. All Rights Reserved.