TY  - JOUR
A1  - Kubatova, Nina
A1  - Pyper, Dennis Joshua
A1  - Jonker, Hendrik R. A.
A1  - Saxena, Krishna
A1  - Remmel, Laura
A1  - Richter, Christian
A1  - Brantl, Sabine
A1  - Evguenieva-Hackenberg, Elena
A1  - Hess, Wolfgang
A1  - Klug, Gabriele
A1  - Marchfelder, Anita
A1  - Soppa, Jörg
A1  - Streit, Wolfgang
A1  - Mayzel, Maxim
A1  - Orekhov, Vladislav Y.
A1  - Fuxreiter, Monika
A1  - Schmitz-Streit, Ruth
A1  - Schwalbe, Harald
T1  - Rapid biophysical characterization and NMR spectroscopy structural analysis of small proteins from bacteria and archaea
T2  - ChemBioChem
N2  - 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.
KW  - NMR spectroscopy
KW  - proteomics
KW  - small proteins
KW  - structural biology
KW  - structure–activity relationships
Y1  - 2019
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/63819
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-638192
SN  - 1439-7633
N1  - This work was supported by the Deutsche Forschungsgemeinschaft (DFG) within the SPP 2002 priority program and the Swedish Research Council (research grant 201504614). Work at BMRZ is supported by the state of Hessen.
VL  - 21
IS  - 8
SP  - 1178
EP  - 1187
PB  - Wiley-VCH
CY  - Weinheim
ER  -