Association energetics of membrane spanning alpha-helices.
Association energetics of membrane spanning alpha-helices.
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DOI：
10.1016/j.sbi.2008.04.007
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发表时间：
2008-08
影响因子：
6.8
通讯作者：
Fleming KG
中科院分区：
文献类型：
--
作者：
MacKenzie KR;Fleming KG
自从Popot和Engelman提出了“两阶段”热力学框架来剖析螺旋膜蛋白折叠的能量学以来，科学家们一直致力于测量螺旋-螺旋缔合的自由能，以更好地了解螺旋之间的相互作用如何稳定和指定天然膜蛋白折叠。用于探测这些能量的主要生物物理工具是沉降平衡分析超离心、荧光共振能量转移和硫醇二硫键交换实验。热力学结果的直接和间接比较表明，胶束和双层之间的螺旋-螺旋稳定性的差异可能不会像以前预期的那么大。遗传学方法继续变得更加定量，并且螺旋在细菌膜中相互作用的倾向通常与体外测量很好地相关。
Since Popot and Engelman proposed the ‘two-stage’ thermodynamic framework for dissecting the energetics of helical membrane protein folding, scientists have endeavored to measure the free energies of helix–helix associations to better understand how interactions between helices stabilize and specify native membrane protein folds. Chief among the biophysical tools used to probe these energies are sedimentation equilibrium analytical ultracentrifugation, fluorescence resonance energy transfer, and thiol disulfide interchange experiments. Direct and indirect comparisons of thermodynamic results suggest that differences in helix–helix stabilities between micelles and bilayers may not be as large as previously anticipated. Genetic approaches continue to become more quantitative, and the propensities for helices to interact in bacterial membranes generally correlate well with in vitro measurements.
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DOI：
10.1073/pnas.83.17.6258
发表时间：
1986-09-01
影响因子：
11.1
作者：
GRASBERGER, B;MINTON, AP;METZGER, H
通讯作者：
METZGER, H
影响因子：
5.6
作者：
Doura, AK;Fleming, KG
通讯作者：
Fleming, KG
影响因子：
2.9
作者：
Duneau, Jean-Pierre;Vegh, Attila P.;Sturgis, James N.
通讯作者：
Sturgis, James N.
影响因子：
5.6
作者：
Fleming, KG
通讯作者：
Fleming, KG
DOI：
10.1073/pnas.0501234102
发表时间：
2005-10-04
影响因子：
11.1
作者：
Kim, S;Jeon, TJ;Bowie, JU
通讯作者：
Bowie, JU