Amylose and amylopectine macromolecules, which have the same chemical nature but a different structure, linear and highly branched, are found (by atomic force microscopy) to adsorb in different conformations on CNT surface, helical and random, respectively.
This is supported by deconvolution and peak fitting of the spectral region including Amide I and II peaks (Fig. 7c, d), which uncovers two main components centred at ~1658 and ~1629 cm−1 corresponding to the helical and random (or uncoiled) components, respectively.
The close proximity of Amide I bands arising from helical and random coil structures makes it difficult to differentiate between these two forms.
Values for dCut and the elastic constants for helical and random coil regions were determined by comparison of the residue fluctuations of a monomeric δOR simulated for 50 ns using the Optimized Potentials for Liquid Simulations-All Atom (OPLS-AA) force field in an explicit POPC/10% cholesterol bilayer with the same quantity obtained from a 50 ns simulation of the CG model.
There are three ribosomal proteins (S5, S8, S10) with hairpin extensions and one (S17) with both helical and hairpin extensions.
The magnitude of this coupling constant in Ser-OGlcNAc strongly suggests a conformationally restricting interaction that is present in both the α-helical and random coil states.
The electrospun gelatin nanofiber exhibited a mixture of α-helical and random coil conformation, which was amorphous structure with very low crystallinity.
The formation of small soluble oligomers is associated with the conformational transition of Aβ from α-helical and random coiled state to a β-sheet structure, as demonstrated by circular dichroism.
The immobilized peptide undergoes a structural transition between α-helical and random coil conformation upon changes in pH and ionic concentration, but critically the threshold for conformational change is altered dramatically by molecular crowding within the peptide monolayer.
Second is the Kabash and Sander representation (34), which highlights the structural motifs for four of the five ligands, with their respective loops, varying length antiparallel β-sheets, short helical motif, and random coil contributions for EGF, TGF- α, HB-EGF, and ER (Fig. 1, B, D, F, and H ), respectively.
