Nina Kubatova, Dennis Joshua Pyper, Hendrik R. A. Jonker, Krishna Saxena, Laura Remmel, Christian Richter, Sabine Brantl, Elena Evguenieva-Hackenberg, Wolfgang Hess, Gabriele Klug, Anita Marchfelder, Jörg Soppa, Wolfgang Streit, Maxim Mayzel, Vladislav Y. Orekhov, Monika Fuxreiter, Ruth Schmitz-Streit, Harald Schwalbe
- 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.
MetadatenAuthor: | Nina Kubatova, Dennis Joshua Pyper, Hendrik R. A. JonkerORCiD, Krishna SaxenaORCiDGND, Laura Remmel, Christian RichterORCiDGND, Sabine Brantl, Elena Evguenieva-Hackenberg, Wolfgang Hess, Gabriele Klug, Anita MarchfelderORCiD, Jörg SoppaORCiD, Wolfgang Streit, Maxim Mayzel, Vladislav Y. Orekhov, Monika Fuxreiter, Ruth Schmitz-StreitORCiDGND, Harald SchwalbeORCiDGND |
---|
URN: | urn:nbn:de:hebis:30:3-638192 |
---|
DOI: | https://doi.org/10.1002/cbic.201900677 |
---|
ISSN: | 1439-7633 |
---|
Parent Title (English): | ChemBioChem |
---|
Publisher: | Wiley-VCH |
---|
Place of publication: | Weinheim |
---|
Document Type: | Article |
---|
Language: | English |
---|
Date of Publication (online): | 2019/11/09 |
---|
Date of first Publication: | 2019/11/09 |
---|
Publishing Institution: | Universitätsbibliothek Johann Christian Senckenberg |
---|
Release Date: | 2022/01/25 |
---|
Tag: | NMR spectroscopy; proteomics; small proteins; structural biology; structure–activity relationships |
---|
Volume: | 21 |
---|
Issue: | 8 |
---|
Page Number: | 10 |
---|
First Page: | 1178 |
---|
Last Page: | 1187 |
---|
Note: | 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. |
---|
HeBIS-PPN: | 49129400X |
---|
Institutes: | Biowissenschaften |
---|
| Wissenschaftliche Zentren und koordinierte Programme / Zentrum für Biomolekulare Magnetische Resonanz (BMRZ) |
---|
Dewey Decimal Classification: | 5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften |
---|
| 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
---|
Sammlungen: | Universitätspublikationen |
---|
Licence (German): | Creative Commons - Namensnennung 4.0 |
---|