Department of Structural and Molecular Biology, Division of Biosciences, University College London, London, WC1E 6BT, United Kingdom.
Department of Structural and Molecular Biology, Division of Biosciences, University College London, London, WC1E 6BT, United Kingdom.
Curr Opin Struct Biol. 2021 Oct;70:61-69. doi: 10.1016/j.sbi.2021.04.002. Epub 2021 May 11.
The surface of proteins is covered by side chains of polar amino acids that are imperative for modulating protein functionality through the formation of noncovalent intermolecular interactions. However, despite their tremendous importance, the unique structures of protein side chains require tailored approaches for investigation by nuclear magnetic resonance spectroscopy and so have traditionally been understudied compared with the protein backbone. Here, we review substantial recent methodological advancements within nuclear magnetic resonance spectroscopy to address this issue. Specifically, we consider advancements that provide new insight into methyl-bearing side chains, show the potential of using non-natural amino acids and reveal the actions of charged side chains. Combined, the new methods promise unprecedented characterisations of side chains that will further elucidate protein function.
蛋白质的表面覆盖着极性氨基酸的侧链，这些侧链对于通过形成非共价的分子间相互作用来调节蛋白质的功能至关重要。然而，尽管它们非常重要，但蛋白质侧链的独特结构需要通过核磁共振波谱学进行专门的研究，因此与蛋白质主链相比，传统上对它们的研究较少。在这里，我们回顾了核磁共振波谱学中解决这个问题的重要的最新方法学进展。具体来说，我们考虑了提供有关甲基侧链新见解的进展，展示了使用非天然氨基酸的潜力，并揭示了带电侧链的作用。总的来说，这些新方法有望对侧链进行前所未有的描述，从而进一步阐明蛋白质的功能。
