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The results presented here and in Reference 8 demonstrate the power of using tethered chemical nucleases to reveal and monitor structural transitions during the course of a macromolecular reaction.
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Lee et al. monitored the structural transitions of α-synuclein as it bound to phospholipid vesicles.
By monitoring the structural transitions of G⊃ACN via rheology, we have established how the conversion into subsequent viscoelastic phase (VE⊃ACN) alters the overall network rigidity.
Order parameters are useful quantities to monitor the structural transition within peptide oligomers [46].
We used multidimensional NMR and circular dichroism spectroscopy to monitor the observed structural transitions, and described the conformational landscapes using statistical ensemble and molecular-dynamics simulations.
The monitored fast structural transition is attributed to the effective vesicle-vesicle interactions between different vesicles or between different lamellae within one vesicle.
In our present study, we carried out stopped-flow experiments combined with synchrotron SAXS for monitoring in-situ the structural transitions in DOPG/MO-based vesicles induced by rapidly added Ca2+ solutions.
Thermally induced structural transitions in the secondary structure monitored by infrared spectroscopy have been previously described [ 39- 42] to analyze the unfolding behavior of proteins and to determine a melting temperature (TmFTIR).
When combined with NMR spectroscopy, hydrostatic pressure offers the possibility to monitor at a residue level the structural transitions occurring upon unfolding and to determine the kinetic properties of the process.
Investigates structural transitions and structure-property relationships through practical materials examples.
The amide III spectral region has the advantage that structural transitions can be monitored easily without spectral deconvolution because the absorptions of α-helix (ca. 1330-1290 cm-1), other, and β-sheet (ca. 1250-1215 cm-1) structure structure are well separated [ 34].
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