random coil


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random coil

[′ran·dəm ′kȯil]
(physical chemistry)
Any of various irregularly coiled polymers that can occur in solution. Also known as cyclic coil.
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The ratio of protein secondary structure (the infrared signal ratio of [beta]-sheet/[alpha]-helix and random coil) was higher in infants than in adults, and the higher ratio of protein secondary structure in infant skin coincides with a higher TEWL value.
[beta]-sheet Random coil PHBV/SF (1610-1640 [cm.sup.-1]) (1645-1665 [cm.sup.-1]) 0/100 61.3% 29.4% 25/75 59.4% 28.2% 50/50 62.7% 27.6% 75/25 59.5% 27.1% TABLE 3.
Random coil is significantly overrepresented in +1, +2, +3, +4, and +5 positions (see Table 2).
This algorithm shows what state (pure random coil or random coil with 3/10 helix) is more probable for a given connecting bridge.
39813.1 39853.2 6612.6 6582.5 pI of Domain 7.76 7.77 5.55 5.55 Half-Life 1.9 hrs 1.9 hrs 30 hrs 30 hrs Instability index 76.06 76.18 44.10 38.14 Hydropathicity -0.466 -0.471 -0.077 -0.120 Alpha helix 12.87% 16.09% 1.64% 0.00% Extended strand 7.77% 7.77% 42.62% 42.62% Beta turn 0.27% 0.27% 4.92% 4.92% Random coil 79.09% 75.87% 50.82% 52.46% Stability Stable unstable unstable stable Features Neogenin_C N M Mol.
At high shear rates, the time allowed for the formation and dissolution of entanglements is very short since the interaction time for two molecules whose random coil dimensions are overlapped is brief.
The rest is sometimes classified as "random coil," but generally, it is neither random nor coiled.
Specifically, the spectra of the bands of 1650~1660,1665~1680, and 1660~1665 [cm.sup.-1] ranges are, respectively, corresponding to [alpha]-helix, [beta]-sheet, and random coil of the protein.
We found that the percentage of random coil structures was positively correlated with PS and digestibility, possibly because this structure is strong and flexible and has fewer hydrogen bonds that can impede enzyme access, which allows proteins to be readily degraded.
This demonstrated SA components obviously existing in the SF/SA hybrid scaffolds, and the crystalline structure of SF was also mainly the random coil structure.
Compared with the control, on the whole, CRL7 exhibited a decrease in [alpha]helix and an increase in [beta]-sheet, [beta]-turn, and random coil (except for xylene and acetonitrile whose [beta]-sheet decreased).
The SF matrix consisted of two main conformations including random coil (water-soluble) and [beta]-sheet (water-insoluble) forms [6].