An efficient combination of BEST and NUS methods in multidimensional NMR spectroscopy for high throughput analysis of proteins.
RSC Adv
; 8(32): 17616-17621, 2018 May 14.
Article
de En
| MEDLINE
| ID: mdl-35542095
ABSTRACT
Application of Non Uniform Sampling (NUS) along with Band-selective Excitation Short-Transient (BEST) NMR experiments has been demonstrated for obtaining the important residue-specific atomic level backbone chemical shift values in short durations of time. This application has been demonstrated with both well-folded (ubiquitin) and unfolded (α-synuclein) proteins alike. With this strategy, the experiments required for determining backbone chemical shifts can be performed very rapidly, i.e., in â¼2 hours of spectrometer time, and this data can be used to calculate the backbone folds of proteins using well established algorithms. This will be of great value for structural proteomic investigations on one hand, where the speed of structure determination is a limiting factor and for application in the study of slow kinetic processes involving proteins, such as fibrillization, on the other hand.
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1
Collection:
01-internacional
Base de données:
MEDLINE
Langue:
En
Journal:
RSC Adv
Année:
2018
Type de document:
Article