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Retro operation on the Trp-cage miniprotein sequence produces an unstructured molecule capable of folding similar to the original only upon 2,2,2-trifluoroethanol addition
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SYSNO ASEP 0438291 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Retro operation on the Trp-cage miniprotein sequence produces an unstructured molecule capable of folding similar to the original only upon 2,2,2-trifluoroethanol addition Author(s) Vymětal, Jiří (UOCHB-X) RID, ORCID
Bathula, S. R. (CZ)
Černý, Jiří (BTO-N) RID, ORCID
Chaloupková, R. (CZ)
Žídek, L. (CZ)
Sklenář, V. (CZ)
Vondrášek, Jiří (UOCHB-X) RID, ORCIDNumber of authors 7 Source Title Protein Engineering Design and Selection - ISSN 1741-0126
Roč. 27, č. 12 (2014), s. 463-472Number of pages 10 s. Language eng - English Country GB - United Kingdom Keywords protein folding ; protein-structure prediction ; molecular dynamics ; NMR methods ; CD spectroscopy Subject RIV CE - Biochemistry R&D Projects LH11020 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GA203/08/0114 GA ČR - Czech Science Foundation (CSF) Institutional support UOCHB-X - RVO:61388963 ; BTO-N - RVO:86652036 UT WOS 000345837300001 DOI https://doi.org/10.1093/protein/gzu046 Annotation Amino acid sequence and environment are the most important factors determining the structure, stability and dynamics of proteins. To evaluate their roles in the process of folding, we studied a retroversion of the well-described Trp-cage miniprotein in water and 2,2,2-trifluoroethanol (TFE) solution. We show, by circular dichroism spectroscopy and nuclear magnetic resonance (NMR) measurement, that the molecule has no stable structure under conditions in which the Trp-cage is folded. A detectable stable structure of the retro Trp-cage, with the architecture similar to that of the original Trp-cage, is established only upon addition of TFE to 30% of the total solvent volume. The retro Trp-cage structure shows a completely different pattern of stabilizing contacts between amino acid residues, involving the guanidinium group of arginine and the aromatic group of tryptophan. The commonly used online prediction methods for protein and peptide structures Robetta and PEP-FOLD failed to predict that the retro Trp-cage is unstructured under default prediction conditions. On the other hand, both methods provided structures with a fold similar to those of the experimentally determined NMR structure in water/TFE but with different contacts between amino acids. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Year of Publishing 2015
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