Hydration shell differentiates folded and disordered states of a Trp-cage miniprotein, allowing characterization of structural heterogeneity by wide-line NMR measurements.
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ABSTRACT:
SUBMITTER: Taricska N
PROVIDER: S-EPMC6393587 | biostudies-literature | 2019 Feb
REPOSITORIES: biostudies-literature
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Hydration shell differentiates folded and disordered states of a Trp-cage miniprotein, allowing characterization of structural heterogeneity by wide-line NMR measurements.
Taricska Nóra N Bokor Mónika M Menyhárd Dóra K DK Tompa Kálmán K Perczel András A
Scientific reports 20190227 1
Hydration properties of folded and unfolded/disordered miniproteins were monitored in frozen solutions by wide-line <sup>1</sup>H-NMR. The amount of mobile water as function of T (-80 °C < T < 0 °C) was found characteristically different for folded (TC5b), semi-folded (pH < 3, TCb5(H+)) and disordered (TC5b_N1R) variants. Comparing results of wide-line <sup>1</sup>H-NMR and molecular dynamics simulations we found that both the amount of mobile water surrounding proteins in ice, as well as their ...[more]
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