The far-UV CD spectra of FXR1 Nt-KH2 and Nt-KH1 and of FMRP Nt-KH1 are typical of well-folded proteins with features of a mixed αβ fold, as we expect from what we know about the structures of the Tudor and KH domains which must contribute to the signal.
It contains the catalytic domain characteristic of class II synthetases, a helical domain with a hairpin motif critical for acceptor-stem recognition, and a C-terminal domain of a mixed α/β fold.
The crystal structure of Sso10b revealed that the monomer has a mixed α/β fold comprising two α-helices and four β-sheets and resembles that of the C-terminal domain of the bacterial translation initiation factor IF3 [16].
The structure of PglB comprises a helical transmembrane domain and a mixed α/β fold periplasmic domain, which share substantial non-covalent interactions and are both required for binding substrates and catalysis.
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Mouse stomatin86 213 has a mixed α/β-fold.
Secondary structure prediction for sAC-HD suggests a mixed α β-fold, and UV–CD spectroscopy indeed indicates approx. 34% α β-foldand 30% β-sheet content.
We systematically investigate small (dihedral angle flips in a protein), large (nucleosome tail collapse and DNA unwrapping), and mixed (folding of a miniprotein) conformational changes, with nominal simulation times ranging from nanoseconds to microseconds depending on system size.
It is found that for hierarchical tubes (HTs) there are three folding styles, including sub-cell folding, mixed folding and global folding.
Table 8 shows the results of simulation 3, a more challenging situation where expression levels varied with mixed fold-changes ranging from as small as less than 1.5 to 4. Furthermore, there were two change points in a non-monotonic trend for each gene in this simulation.
