Mannige Ranjan
The Multiscale Institute, Berkeley Lake, GA, USA.
PeerJ. 2018 Oct 16;6:e5745. doi: 10.7717/peerj.5745. eCollection 2018.
Protein backbones occupy diverse conformations, but compact metrics to describe such conformations and transitions between them have been missing. This report re-introduces the Ramachandran number (ℛ) as a residue-level structural metric that could simply the life of anyone contending with large numbers of protein backbone conformations (e.g., ensembles from NMR and trajectories from simulations). Previously, the Ramachandran number (ℛ) was introduced using a complicated closed form, which made the Ramachandran number difficult to implement. This report discusses a much simpler closed form of ℛ that makes it much easier to calculate, thereby making it easy to implement. Additionally, this report discusses how ℛ dramatically reduces the dimensionality of the protein backbone, thereby making it ideal for simultaneously interrogating large numbers of protein structures. For example, 200 distinct conformations can easily be described in one graphic using ℛ (rather than 200 distinct Ramachandran plots). Finally, a new Python-based backbone analysis tool-BackMAP-is introduced, which reiterates how ℛ can be used as a simple and succinct descriptor of protein backbones and their dynamics.
蛋白质主链具有多种构象,但一直缺少用于描述这些构象及其之间转变的简洁度量。本报告重新引入了拉马钱德兰数(ℛ),作为一种残基水平的结构度量,它可以简化任何处理大量蛋白质主链构象(例如,来自核磁共振的系综和模拟轨迹)的人的工作。以前,拉马钱德兰数(ℛ)是用一种复杂的封闭形式引入的,这使得拉马钱德兰数难以实现。本报告讨论了一种简单得多的ℛ封闭形式,使其计算变得容易得多,从而便于实现。此外,本报告还讨论了ℛ如何极大地降低了蛋白质主链的维度,从而使其非常适合同时研究大量蛋白质结构。例如,使用ℛ可以在一张图中轻松描述200种不同的构象(而不是200个不同的拉马钱德兰图)。最后,介绍了一种基于Python的新的主链分析工具——BackMAP,它再次强调了ℛ如何可以用作蛋白质主链及其动力学的简单而简洁的描述符。