random coil


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random coil

n.
A protein structure characterized by irregular coils or folds.
References in periodicals archive ?
The secondary structure prediction of Anxa2 protein indicated that 46.61% alpha helix, 14.75% extended chain, and 38.64% random coil might be formed (Figure 2).
Therefore, the secondary structure of FK had been changed, and some random coil structures also had been into [beta]-sheet structure in the preparation process of FK-GlyM.
[18]: the bands located at 1650-1660 [cm.sup.-1] were assigned to the [alpha]-helix, the bands located at 1618-1640 [cm.sup.-1] and 1670-1690 [cm.sup.-1] were assigned to the [beta]-sheet, the bands at 1660-1670 [cm.sup.-1] and 1690-1700 [cm.sup.-1] were assigned to [beta]-turns, and the band at 1645 [cm.sup.-1] was assigned to random coils. The results of the curve fitting procedure (Table 4) show that the predominant secondary structure in the dough was the [beta]-sheet conformation (about 50%), as found by other authors [18], followed by [beta]-turn and [alpha]-helix and random coil conformation.
The amount of sebum with an ester bond and the index of protein secondary structure ([beta]/[alpha] defined by the signal ratio of [alpha]-helix and random coil and [beta]-sheet) were measured using a Fourier Transform Infrared (FT-IR) Spectrometer (Flexscan, A2 Technologies, Santa Clara, United States), and average values from more than 3 measurements for each body site were calculated.
The salt soluble collagen is basically uncross-linked tropocollagen random coils, which is testified by the CD spectra that clearly shows the random coil orientation of the isolated collagen (Fig.
It is reported that SF can be a random coil structure or two kinds of crystalline structures, Silk I and Silk II [32], Silk I is the metastable structure of fibroin obtained in the abdominal glands of B.
In a good solvent, the resin usually is in a random coil configuration with an 'a' of 0.4-0.7.
This should be attributed to the DNA molecule exhibiting a random coil conformation instead of a compacted spherical particle conformation.
The usage of sheet-like pentapeptides grows in alpha helices and in random coil due to mutational GC-pressure [14].
It has been shown that random coil regions can be considered to function as "connecting bridges" between major elements of secondary structure (alpha helices and beta strands) [12].
The keratin/galactose and sucrose blend films indicated the absorption peaks at about 1700 [cm.sup.-1] resulted to the random coil deformation structure.
A[sz]s are amphiphilic peptides with a hydrophilic N-terminal domain (residues 1 to 28) and a hydrophobic C-terminal (residues 29 to 40-42), the latter corresponding to a part of the transmembrane domain of APP.4 ?-Amyloid assembly into fibrils is initiated by a conformational transition from random coil to ?-sheet (hence the name ?-amyloid) and a nucleation-dependent aggregation process.4 A?