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Rapid Biophysical Characterization and NMR Spectroscopy Structural Analysis of Small Proteins from Bacteria and Archaea

Artikel i vetenskaplig tidskrift
Författare Nina Kubatova
Dennis J. Pyper
Hendrik R.A. Jonker
Krishna Saxena
Laura Remmel
Christian Richter
Sabine Brantl
Elena Evguenieva-Hackenberg
Wolfgang R. Hess
Gabriele Klug
Anita Marchfelder
Jörg Soppa
Wolfgang Streit
Maxim Mayzel
Vladislav Orekhov
Monika Fuxreiter
Ruth A. Schmitz
Harald Schwalbe
Publicerad i ChemBioChem
Volym 21
Nummer/häfte 8
Sidor 1178-1187
ISSN 1439-4227
Publiceringsår 2020
Publicerad vid Svenskt NMR-centrum vid Göteborgs universitet
Institutionen för kemi och molekylärbiologi
Sidor 1178-1187
Språk en
Länkar https://doi.org/10.1002/cbic.201900...
Ämnesord NMR spectroscopy, proteomics, small proteins, structural biology, structure–activity relationships
Ämneskategorier Strukturbiologi, Biokemi, Molekylär biofysik

Sammanfattning

© 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. Proteins encoded by small open reading frames (sORFs) have a widespread occurrence in diverse microorganisms and can be of high functional importance. However, due to annotation biases and their technically challenging direct detection, these small proteins have been overlooked for a long time and were only recently rediscovered. The currently rapidly growing number of such proteins requires efficient methods to investigate their structure–function relationship. Herein, a method is presented for fast determination of the conformational properties of small proteins. Their small size makes them perfectly amenable for solution-state NMR spectroscopy. NMR spectroscopy can provide detailed information about their conformational states (folded, partially folded, and unstructured). In the context of the priority program on small proteins funded by the German research foundation (SPP2002), 27 small proteins from 9 different bacterial and archaeal organisms have been investigated. It is found that most of these small proteins are unstructured or partially folded. Bioinformatics tools predict that some of these unstructured proteins can potentially fold upon complex formation. A protocol for fast NMR spectroscopy structure elucidation is described for the small proteins that adopt a persistently folded structure by implementation of new NMR technologies, including automated resonance assignment and nonuniform sampling in combination with targeted acquisition.

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