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• W2160520240 abstract "Protein NMR spectroscopy has expanded dramatically over the last decade into a powerful tool for the study of their structure, dynamics, and interactions. The primary requirement for all such investigations is sequence-specific resonance assignment. The demand now is to obtain this information as rapidly as possible and in all types of protein systems, stable/unstable, soluble/insoluble, small/big, structured/unstructured, and so on. In this context, we introduce here two reduced dimensionality experiments – (3,2)D-hNCOcanH and (3,2)D-hNcoCAnH – which enhance the previously described 2D NMR-based assignment methods quite significantly. Both the experiments can be recorded in just about 2-3 h each and hence would be of immense value for high-throughput structural proteomics and drug discovery research. The applicability of the method has been demonstrated using alpha-helical bovine apo calbindin-D9k P43M mutant (75 aa) protein. Automated assignment of this data using AUTOBA has been presented, which enhances the utility of these experiments. The backbone resonance assignments so derived are utilized to estimate secondary structures and the backbone fold using Web-based algorithms. Taken together, we believe that the method and the protocol proposed here can be used for routine high-throughput structural studies of proteins." @default.
• W2160520240 created "2016-06-24" @default.
• W2160520240 creator A5017392244 @default.
• W2160520240 creator A5037894792 @default.
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• W2160520240 date "2014-09-01" @default.
• W2160520240 modified "2023-09-28" @default.
• W2160520240 title "Reduced dimensionality (3,2)D NMR experiments and their automated analysis: implications to high-throughput structural studies on proteins" @default.
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• W2160520240 doi "https://doi.org/10.1002/mrc.4135" @default.
• W2160520240 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25178811" @default.
• W2160520240 hasPublicationYear "2014" @default.
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