Hydrophobicity--shake flasks, protein folding and drug discovery.
Hydrophobicity--shake flasks, protein folding and drug discovery.
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DOI：
10.2174/156802610790232233
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发表时间：
2010
影响因子：
3.4
通讯作者：
Kellogg GE
中科院分区：
文献类型：
--
作者：
Sarkar A;Kellogg GE
疏水相互作用是自然界中一些最重要的相互作用。它们是许多现象的主要驱动力。这主要是一种熵效应，可以解释许多生物物理事件，例如在药物设计中非常重要的蛋白质-蛋白质或蛋白质-配体结合。对这种现象的最早研究可以追溯到 19 世纪末，当时 Meyer 和 Overton 独立地将气体的疏水性与其麻醉效力相关联。从那时起，这一科学领域取得了重大进展。本文简要回顾了疏水性研究的历史以及分配系数的理论估计。最后讨论了疏水性估计方法在药物设计和蛋白质折叠领域的应用。
Hydrophobic interactions are some of the most important interactions in nature. They are the primary driving force in a number of phenomena. This is mostly an entropic effect and can account for a number of biophysical events such as protein-protein or protein-ligand binding that are of immense importance in drug design. The earliest studies on this phenomenon can be dated back to the end of the 19th century when Meyer and Overton independently correlated the hydrophobic nature of gases to their anesthetic potency. Since then, significant progress has been made in this realm of science. This review briefly traces the history of hydrophobicity research along with the theoretical estimation of partition coefficients. Finally, the application of hydrophobicity estimation methods in the field of drug design and protein folding is discussed.
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影响因子：
7.3
作者：
Cozzini, P;Fornabaio, M;Mozzarelli, A
通讯作者：
Mozzarelli, A
影响因子：
7.3
作者：
Amadasi, Alessio;Surface, J. Andrew;Kellogg, Glen E.
通讯作者：
Kellogg, Glen E.
影响因子：
5.6
作者：
CASARI, G;SIPPL, MJ
通讯作者：
SIPPL, MJ
影响因子：
3.5
作者：
ABRAHAM, DJ;KELLOGG, GE
通讯作者：
KELLOGG, GE
DOI：
10.1002/qsar.19900090302
发表时间：
1990-09-01
期刊：
QUANTITATIVE STRUCTURE-ACTIVITY RELATIONSHIPS
影响因子：
--
作者：
AKAMATSU, M;OKUTANI, S;FUJITA, T
通讯作者：
FUJITA, T