random coil


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ran·dom coil

a structure of a macromolecule (typically, a biopolymer) that changes over time.
Farlex Partner Medical Dictionary © Farlex 2012

random coil

n.
A protein structure characterized by irregular coils or folds.
The American Heritage® Medical Dictionary Copyright © 2007, 2004 by Houghton Mifflin Company. Published by Houghton Mifflin Company. All rights reserved.
References in periodicals archive ?
Alpha helix, extended strand, random coil are indicated, respectively, with the longest, the second longest, the third longest.
The characteristic peaks of random coil structure of FK appeared at near 195 nm while the characteristic peaks of [beta]-sheet layer structure of FK-Gly[Cu.sub.x] complex appeared in the vicinity of 200 nm.
reported that the SC barrier functional deficiency in psoriatic skin is accompanied by a change of SC protein secondary structure (ratio of [beta]-sheet/[alpha]-helix and random coil) measured using FT-IR [15].
FTIR spectroscopy is a frequently used method to monitor the secondary structure of SF [37], The absorption bands observed for SF at 1655 [+ or -] 10 [cm.sup.-1] (amide I) and 1540 [+ or -] 10 [cm.sup.-1] (amide II) are assigned to random coil structure.
Yoshikawa, "Transition of double-stranded DNA chains between random coil and compact globule states induced by cooperative binding of cationic surfactant," Journal of the American Chemical Society, vol.
Average usages of Lys and Arg have been calculated near binding and nonbinding glutamic acid residues being in alpha helix, beta strand, and random coil.
The aim of the present study was to compare 3/10 helices with random coil structures.
Keratin/galactose and sucrose comprised of the mixture structure of [alpha]-helix and random coil deformation while the structure of keratin/starch blend film was [alpha]-helix mixed [beta]-sheet structure.
wt., pi of domain, half-life, instability index, hydropathicity, alpha helix, extended strand, beta turn, random coil stability, analysis of domains were performed and it was observed that mutation of single amino acid has a great affect on the domain structure and stability (Table 3).
With large strains and rates of deformation, there are large displacements of the polymer chains from the random coil configurations central to the molecular theories that describe linear viscoelastic behavior.
The best estimates of secondary structure proportions obtained from the far UV data for the native Ara h2 were 18.2% of the molecule in [alpha]-helices, 54% in [beta]-pleated sheets, and 27.7% in a random coil configuration.
Molecular dynamics results, which reproduce the measured quasielastic neutron spectra extremely well, show that the observed dynamic changes arise primarily from the particular region of the protein that forms a beta sheet in the native state and unfolds to a random coil in the molten globule.