Exact(1)
PEPstr uses β-turns and secondary structure (Helix, Sheet, Coil) information predicted using BetaTurns and PSIPRED software respectively [ 44, 49].
Similar(59)
We then acquired a Circular Dichroism (CD) spectrum to study the secondary structure of freshly prepared hPRM1 peptide solution, which displays a clear minimum at 220 nm, indicating that synthetic hPRM1 adopts a structure rich in random coil (Supporting Information, Figure S3A).
To test whether coiled-coil regions carry phylogenetic information, we measured sequence conservation of coiled-coil regions and compared it with globular domains in a collection of over 2,000 orthologous groups of metazoan proteins.
Backbone Cα NMR chemical shift indices (CSI, the difference between the observed chemical shift and shifts observed for random coil structures) provide information on local secondary structure [34], [35], with downfield shifts (positive deviations) reflecting α-helical conformations and upfield shifts reflecting extended (β-strand) conformations.
Twelve different DNA-coil solutions containing different amounts of VC and EC DNA-coils (see Supporting information, Table S2) were prepared according to the following protocol: VC and EC ligation mixes (200 μL, 20 nM) were prepared separately according to the procedure in the previous section (scaled up 4 times, target and padlock sequences according to Supporting information, Table S1).
Finally, we showed that coiled-coils contain valuable sequence information that can be used in homology detection and that homology detection can be improved by using the CC model.
Here we overcome this limitation by attaching a beam of soft elastomer to the functional fiber, thereby creating a composite system which exhibits in-drop coiling and carries information while being ultra-extensible.
When measuring on samples with only 250-nm beads and EC-coils (see Supporting information, Fig. S3A), the free-bead peak is located at 15 Hz, whereas the free-bead peak for 100-nm beads (see Supporting information, Fig. S3B) is located at 40 Hz.
We used the underlying information contained within coiled-coil regions to develop a new model that both describes evolutionary patterns in coiled-coil sequences and provides an improvement over more general models; one should consider using the CC model to improve the toolkit used in the classical phylogenetic analysis pipeline for coiled-coil proteins.
This technique relies on the fact that the signal from a multi-element surface coil contains limited spatial information because of the differing sensitivities of the component coils.
For instance, a tightly coiled corkscrew may carry different information from a loosely coiled one, resulting in a different pattern captured by the receiver (see image).
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