Steered molecular dynamics investigations of protein function
Steered molecular dynamics investigations of protein function
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DOI：
10.1016/s1093-3263(00)00133-9
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发表时间：
2001-01-01
影响因子：
2.9
通讯作者：
Schulten, K
中科院分区：
文献类型：
--
作者：
Isralewitz, B;Baudry, J;Schulten, K
蛋白质的分子识别和机械特性控制着细胞中可能导致疾病的分子过程，并成为药物设计的目标。单分子测量技术拥有非常先进的知识，但无法解析足够的细节来解释蛋白质结构。我们寻求通过所谓的引导分子动力学（SMD）模拟来补充观察结果，该模拟直接与实验联系起来，并提供潜在事件的原子级描述。我们小组已经启动了这样的研究计划，例如，涉及免疫球蛋白和纤连蛋白结构域的弹性特性以及生物素和亲和素的结合的研究。在本文中，我们解释了 SMD 方法，并提出了如何将其应用于现代分子生物学研究焦点的三个系统的功能：肌肉蛋白肌联蛋白和细胞外基质蛋白纤连蛋白的力转导、抗体-抗原桶的识别以及 K+ 通道的离子选择性传导。 (C) 2001 年，爱思唯尔科学公司。
Molecular recognition and mechanical properties of proteins govern molecular processes in the cell that can cause disease and call be targeted for drug design. Single molecule measurement techniques have greatly advanced knowledge but cannot resolve enough detail to be interpreted in terms of protein structure. We seek to complement the observations through so-called Steered Molecular Dynamics (SMD) simulations that link directly to experiments and provide atomic-level descriptions of the underlying events. Such a research program has been initiated in our group and has involved for example, studies of elastic properties of immunoglobulin and fibronectin domains as well as the binding of biotin and avidin. In this article we explain the SMD method and suggest how it can be applied to the function of three systems that ale the focus of modern molecular biology research: force transduction by the muscle protein titin and extracellular matrix protein fibronectin, recognition of antibody-antigene pails, and ion selective conductivity of the K+ channel. (C) 2001 by Elsevier Science Inc.