Protein structure determination from NMR chemical shifts
Protein structure determination from NMR chemical shifts
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DOI：
10.1073/pnas.0610313104
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发表时间：
2007-06-05
影响因子：
11.1
通讯作者：
Vendruscolo, Michele
中科院分区：
文献类型：
--
作者：
Cavalli, Andrea;Salvatella, Xavier;Vendruscolo, Michele
核磁共振光谱在确定蛋白质和其他生物大分子的结构和动力学方面发挥着重要作用。化学位移是最容易和准确测量的NMR参数，它们非常特异地反映了蛋白质的天然和非天然状态的构象。我们表明，使用11个例子的蛋白质代表的主要结构类别，并含有多达123个残基，它是可能的，使用化学位移作为结构的限制，结合传统的分子力学力场，以确定蛋白质的构象在2埃或更好的分辨率。这一战略应该是广泛适用的，并受到进一步发展，将使定量结构分析进行，以解决一系列复杂的生物学问题，目前的结构技术无法访问。
NMR spectroscopy plays a major role in the determination of the structures and dynamics of proteins and other biological macromolecules. Chemical shifts are the most readily and accurately measurable NMR parameters, and they reflect with great specificity the conformations of native and nonnative states of proteins. We show, using 11 examples of proteins representative of the major structural classes and containing up to 123 residues, that it is possible to use chemical shifts as structural restraints in combination with a conventional molecular mechanics force field to determine the conformations of proteins at a resolution of 2 angstrom or better. This strategy should be widely applicable and, subject to further development, will enable quantitative structural analysis to be carried out to address a range of complex biological problems not accessible to current structural techniques.