- Retro operation on the Trp-cage miniprotein sequence produces an unst…
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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

  1. 1.
    SYSNO0438291
    TitleRetro 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) [690/69] 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) [690/69] RID, ORCID
    Corespondence/seniorVondrášek, Jiří - Korespondující autor
    Source Title Protein Engineering Design and Selection. Roč. 27, č. 12 (2014), s. 463-472
    Document TypeČlánek v odborném periodiku
    Grant LH11020 GA MŠMT - Ministry of Education, Youth and Sports (MEYS), CZ - Czech Republic
    GA203/08/0114 GA ČR - Czech Science Foundation (CSF)
    LO1214, CZ - Czech Republic
    LM2010005, CZ - Czech Republic
    ED1.1.00/02.0068, CZ - Czech Republic
    Institutional supportUOCHB-X - RVO:61388963 ; BTO-N - RVO:86652036
    Languageeng
    CountryGB
    Keywords protein folding * protein-structure prediction * molecular dynamics * NMR methods * CD spectroscopy
    Cooperating institutions Masarykova univerzita Brno (Czech Republic)
    Permanent Linkhttp://hdl.handle.net/11104/0241840
     
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