Automated assignment of methyl NMR spectra from large proteins
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Date
2020
Publication Type
Journal Article
ETH Bibliography
yes
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Abstract
As structural biology trends towards larger and more complex biomolecular targets, a detailed understanding of their interactions and underlying structures and dynamics is required. The development of methyl-TROSY has enabled NMR spectroscopy to provide atomic-resolution insight into the mechanisms of large molecular assemblies in solution. However, the applicability of methyl-TROSY has been hindered by the laborious and time-consuming resonance assignment process, typically performed with domain fragmentation, site-directed mutagenesis, and analysis of NOE data in the context of a crystal structure. In response, several structure-based automatic methyl assignment strategies have been developed over the past decade. Here, we present a comprehensive analysis of all available methods and compare their input data requirements, algorithmic strategies, and reported performance. In general, the methods fall into two categories: those that primarily rely on inter-methyl NOEs, and those that utilize methyl PRE- and PCS-based restraints. We discuss their advantages and limitations, and highlight the potential benefits from standardizing and combining different methods.
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Publication status
published
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Journal / series
Volume
118-119
Pages / Article No.
54 - 73
Publisher
Elsevier
Event
Edition / version
Methods
Software
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Date collected
Date created
Subject
methyl-TROSY; Automatic resonance assignment; Large proteins; Molecular machines
Organisational unit
03782 - Riek, Roland / Riek, Roland