ChemInform Abstract: Validation of Structural Proposals by Substructure Analysis and ¹³C NMR Chemical Shift Prediction.

Abstract

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Random mutagenesis of the nucleotide‐binding domain of NRC1 (NB‐LRR Required for Hypersensitive Response‐Associated Cell Death‐1), a downstream signalling nucleotide‐binding, leucine‐rich repeat (NB‐LRR) protein, identifies gain‐of‐function mutations in the nucleotide‐binding pocket

“…The complete amino acid sequence of NRC1 was used to delineate protein domains with the domain linker predictor (Miyazaki et al ., ), whereas motifs and patterns were assessed with pfam (Finn et al ., ) and Prosite (Sigrist et al ., ). Overall, the prediction of the secondary structure was based on the consensus of several secondary structure prediction methods: gor iv (Garnier et al ., ), hnn (Guermeur & Gallinari, ), sopma (Geourjon & Deleage, ), porter (Pollastri & McLysaght, ), jpred (Cole et al ., ), psipred (Buchan et al ., ), jufo (Meiler et al ., ), sspro (Cheng et al ., ) and sspro8 (Pollastri & Baldi, ). Propensities of the three aspects of intrinsic disorder – coils, missing coordinates and a high B‐factor – were assessed with disembl (Linding et al ., ), iupred (Dosztányi et al ., ) and disopred (Ward et al ., ) and translated into a disorder score for each amino acid position in the sequence.…”