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

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F14%3A00074482" target="_blank" >RIV/00216224:14740/14:00074482 - isvavai.cz</a>
Alternative codes found
RIV/86652036:_____/14:00438291 RIV/61388963:_____/14:00438291
Result on the web
<a href="http://peds.oxfordjournals.org/content/27/12/463.full.pdf+html" target="_blank" >http://peds.oxfordjournals.org/content/27/12/463.full.pdf+html</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/protein/gzu046" target="_blank" >10.1093/protein/gzu046</a>

Result language
angličtina
Original language name
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
Original language description
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 stablestructure 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 stabilizingcontacts between amino acid residues, involving the guanidinium group of arginine and the aromatic group of tryptophan.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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