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Polymer conformation in which all bonded subunits are oriented randomly
In polymer chemistry, a random coil is a conformation of polymers where the monomer subunits are oriented randomly while still being bonded to adjacent
Random_coil
Protocol in biochemistry
Random coil index (RCI) predicts protein flexibility by calculating an inverse weighted average of backbone secondary chemical shifts and predicting values
Random_coil_index
General three-dimensional form of local segments of proteins
flexible loops link the more "regular" secondary structure elements. The random coil is not a true secondary structure, but is the class of conformations
Protein_secondary_structure
Substance composed of macromolecules with repeating structural units
condition), the polymer behaves like an ideal random coil. The transition between the states is known as a coil–globule transition. Inclusion of plasticizers
Polymer
fraction of the molecule in an alpha helix conformation versus turn or random coil. The main attraction in investigating alpha helix formation is that one
Helix–coil_transition_model
Change of a linear protein chain to a 3D structure
ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits
Protein_folding
segments. Further, models group these sections into two broad categories: coils, random conglomerations of disparate unbound pieces, are represented by the
Zimm–Bragg_model
Electrical resonant transformer circuit invented by Nikola Tesla
A Tesla coil is an electrical resonant transformer device designed by inventor Nikola Tesla in 1891. It is used to produce high voltage, low current, high
Tesla_coil
Study of how temperature affects the nucleic acid structure
defined as the temperature at which half of the DNA strands are in the random coil or single-stranded (ssDNA) state. Tm depends on the length of the DNA
Nucleic_acid_thermodynamics
Protein without a fixed 3D structure
IDPs range from fully unstructured to partially structured and include random coil, molten globule-like aggregates, or flexible linkers in large multi-domain
Intrinsically disordered proteins
Intrinsically_disordered_proteins
Protein family
(SNAP-25) is composed of two α-helical domains connected by a random coil linker. The random coil linker region is most notable for its four cysteine residues
SNARE_protein
Polymer with rubber-like elastic properties
elasticity is entropy-driven. In an unstressed state, polymer chains assume random coiled configurations (maximum entropy). Stretching forces the chains into
Elastomer
Region within a prokaryotic cell containing genetic material
additional factors; at thermal equilibrium, it assumes a random coil form. The random coil of E. coli chromosomal DNA would occupy a volume (4/3 π r3)
Nucleoid
Idealization in polymer thermodynamics
the random walk model, where each step taken in a random direction is independent of the directions taken in the previous steps, forming a random coil. The
Kuhn_length
Polymer derived from more than one species of monomer
in different environments. Some conformations that SMA can take are random coil formation, compact globular formation, micelles, and nanodiscs. SMA has
Copolymer
Protein folding hypothesis
well is shown as relatively flat to represent the heterogeneity of the random coil state. The theory's name derives from an analogy between the shape of
Folding_funnel
Type of secondary structure of proteins
α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the
Alpha_helix
Loss of structure in proteins and nucleic acids due to external stress
patterns such as alpha-helices and beta-pleated sheets, and adopt a random coil configuration. Primary structure, such as the sequence of amino acids
Denaturation_(biochemistry)
Chemistry subdiscipline
awarded the Nobel Prize in Chemistry in 1974 for his work on polymer random coil configurations in solution in the 1950s. Stephanie Kwolek developed an
Polymer_chemistry
polymer science, the Lifson–Roig model is a helix-coil transition model applied to the alpha helix-random coil transition of polypeptides; it is a refinement
Lifson–Roig_model
Laboratory technique
as the type of protein secondary structure (beta strands, helices and random coil regions) found in proteins using only backbone chemical shift data The
Chemical_shift_index
Protein produced by silkworms
acids, of which 32% is serine. The secondary structure is usually a random coil, but it can also be easily converted into a β-sheet conformation, via
Sericin
Amino acid
tight coiling of the collagen triple helix. Glycine disrupts the formation of alpha-helices in secondary protein structure, in favor instead of random coils
Glycine
Topics referred to by the same term
Guadeloupe Radio Caribbean International, a radio station in St. Lucia Random coil index, a predictor of protein flexibility Rapid Continuous Improvement
RCI
Manufacture of electromagnetic coils
In electrical engineering, coil winding is the manufacture of electromagnetic coils. Coils are used as components of circuits, and to provide the magnetic
Coil_winding_technology
Polarization state
its respective molecules. Therefore, the alpha helix, beta sheet and random coil regions of proteins and the double helix of nucleic acids have CD spectral
Circular_polarization
Entropy associated with a molecule's possible conformations
probability of the occupancy of that structure. The entropy of heterogeneous random coil or denatured proteins is significantly higher than that of the tertiary
Conformational_entropy
Vegetable gum from the guar bean, Cyamopsis tetragonoloba
is strongly shear-thinning. The rheology of guar gum is typical for a random coil polymer. It does not show the very high low[clarification needed] shear
Guar_gum
Protein family
microorganisms, parasites and some viruses. In water, stomoxyn has a flexible random coil in structure, while in trifluoroethanol it adopts a stable helical structure
Stomoxyn
Protein-coding gene in the species Homo sapiens
the protein forms alpha-helices, 15% forms beta-strands, and 60% is random coil. The various DUF domains are predicted to have variable structure. DUF3699
TASOR2
Partially-folded protein state
ending at the native state. Although often considered a statistical random coil, the denatured state can retain residual structure that mediates (re)folding
Molten_globule
Three-dimensional arrangement of atoms in an amino acid-chain molecule
do not form any regular structures. They should not be confused with random coil, an unfolded polypeptide chain lacking any fixed three-dimensional structure
Protein_structure
Calcium-binding protein
active protein is not highly structured, more than 50% of it adopting a random coil conformation. When calcium binds there is a structural change whereby
Calsequestrin
Analytical technique
complexes: evidence of their wormlike conformation by treating them as random coil polymers". Colloid and Polymer Science. 287 (8): 1001–1004. doi:10
SDS-PAGE
Study of how proteins move and change shape
potentially disordered regions of a protein can be detected using the random coil index. Flexibility in folded proteins can be identified by analyzing
Protein_dynamics
Distributed computing project simulating protein folding
difficult. Moreover, as protein folding is a stochastic process (i.e., random) and can statistically vary over time, it is challenging computationally
Folding@home
Dichroism with circularly polarized light
structural elements such as the alpha-helix, beta-sheet, beta-turn, and random coil. These structural assignments place important constraints on the possible
Circular_dichroism
Technique for determining size distribution of particles
same manner as the scatterer. So, for example, if the scatterer is a random coil polymer, the determined size is not the same as the radius of gyration
Dynamic_light_scattering
Type of transformer
An induction coil or "spark coil" (archaically known as an inductorium or Ruhmkorff coil after Heinrich Rühmkorff) is a type of transformer used to produce
Induction_coil
Process in mitosis and meiosis
Rather, it involves the organized folding of chromatin, initially in a random-coil–like state, into a highly structured rod-shaped form. This structural
Chromosome_condensation
Method for separation and analysis of biomolecules using agarose gel
which treats the polymer matrix as a sieve. A globular protein or a random coil DNA moves through the interconnected pores, and the movement of larger
Agarose_gel_electrophoresis
Variation in resonant frequency of identical atomic nuclei in a magnetic field
of nucleic acids Nuclear magnetic resonance spectroscopy of proteins Random coil index Relaxation (NMR) Solid-state NMR TRISPHAT, a chiral shift reagent
Chemical_shift
Interdisciplinary research area
functional three-dimensional structure from a random coil. Each protein exists as an unfolded polypeptide or random coil when translated from a sequence of mRNA
Molecular_biophysics
Increase of absorbance (optical density) of a material
double helix then separates into two single strands which are in the random coiled conformation. At this time, the base-base interaction will be reduced
Hyperchromicity
Insect protein
energy is lost as heat). It does not have any regular structure but its randomly coiled chains are crosslinked by di- and tri-tyrosine links at the right spacing
Resilin
Concept in molecular modelling
therefore may not require as large a box, as simulations that begin from a random coil conformation. However, the effects of solvation shells on the observed
Periodic_boundary_conditions
Dynamics of fluids confined in nanoscale structures
from a virus have lengths of approx. 100–200 kilobases and will form a random coil of the radius some 700 nm in aqueous solution at 20%. This is also several
Nanofluidics
Surgical treatment for aneurysm
Endovascular coiling is an endovascular treatment for intracranial aneurysms and bleeding throughout the body. The procedure reduces blood circulation
Endovascular_coiling
Amino acid substitutions that mimic a phosphorylated protein
Gerald; Okon, Mark; McIntosh, Lawrence P. (November 2014). "pH-dependent random coil 1H, 13C, and 15N chemical shifts of the ionizable amino acids: a guide
Phosphomimetics
Property of crosslinked rubber
return to its equilibrium or unstretched state, such as a high entropy random coil configuration, once the external force is removed. This is the reason
Rubber_elasticity
Swiss chemist (1919–2012)
investigating decoiling of a random coiled chain molecule in a flowing viscous solvent. Werner Kuhn suggested him to replace the random coil by a dumbbell-model
Hans_Kuhn_(chemist)
Analytical technique
protein, but instead, through a conformational change to a combination of random coil and α helix secondary structures. When a protein mixture is heated to
Polyacrylamide gel electrophoresis
Polyacrylamide_gel_electrophoresis
DNA located in cellular organelles called chloroplasts
glutamic acid. In an aqueous solution, the transit sequence forms a random coil. Not all chloroplast proteins include a N-terminal cleavable transit
Plastid_DNA
Method of prediction of secondary structure of protein
method analyzes sequences to predict alpha helix, beta sheet, turn, or random coil secondary structure at each position based on 17-amino-acid sequence
GOR_method
Protein allowing tissue in the body to resume shape after stretching
consists of a string of 36 small domains, each weighing about 2 kDa in a random coil conformation. The protein consists of alternating hydrophobic and hydrophilic
Elastin
Protein-coding gene in the species Homo sapiens
that has a high lysine content (15%). Most of the protein exists in a random coil structure but the final thirds contains 6 predicted alpha helices. KIAA1257
CFAP92
Most abundant structural protein in animals
secondary structure to the normal collagen polyproline II (PPII) of random coils. This process describes the formation of gelatin, which is used in many
Collagen
Categories of protein tertiary structure
of states from fully unstructured to partially structured and include random coils, (pre-)molten globules, and large multi-domain proteins connected by
Protein_fold_class
Type of biological prediction
not be confused with disordered or unfolded segments of proteins or random coil, an unfolded polypeptide chain lacking any fixed three-dimensional structure
Protein_structure_prediction
Paralyzing neurotoxic peptide
sodium channels. Furthermore, the structure of the peptide shifts from a random coil to the structured helix-turn-helix when introduced to a lipid bilayer
Poneratoxin
Polysaccharide
linked at the 1,3 and 1,4 carbon sites. Oat β-glucans can form into a random coil structure and flow with Newtonian behaviour until they reach a critical
Oat_beta-glucan
Protein-coding gene in the species Homo sapiens
and SNAP-25 associate and begin to wrap around each other to form a coiled coil quaternary structure. The α-helices of both synaptobrevin and syntaxin-1
SNAP25
Early synthetic polymer developed as a textile fiber
are amorphous solids or viscous fluids in which the chains approximate random coils. Below Tm, amorphous regions alternate with regions which are lamellar
Nylon
orientation and the polymer backbone can relax into (the more favored) random coil conformation. That can lead to a macroscopic, reversible deformation
Liquid_crystalline_elastomer
Chemical compound
almost all proteins lose their entire secondary structure and become randomly coiled peptide chains. [citation needed] Guanidinium thiocyanate is also used
Guanidine
Prediction of protein structures
"Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins". Biochemistry. 13 (2): 211–222. doi:10
Chou–Fasman_method
Part of a cathode ray tube which moves the electron beam around
the deflection coil may include ferrite segments to help direct and concentrate the magnetic field. Dismounted deflection yoke coil of a black and white
Deflection_yoke
Protein-coding gene in the species Homo sapiens
TNRC18 consists of 32.61% alpha helix, 6.74% extended strand, and 60.55% random coil. This was found using the GOR4 program available at PRABI-Lyon-Gerland
Trinucleotide repeat containing 18
Trinucleotide_repeat_containing_18
Canadian bioinformatician (born 1961)
could be used to easily and rapidly measure protein flexibility via the random coil index or RCI. Later, he showed how it was possible to use chemical shifts
David_S._Wishart
publications in polymer physics Persistence length Polymer characterization Random coil Worm-like chain H.R Allcock; F.W. Lampe; J.E Mark, Contemporary Polymer
Path integrals in polymer science
Path_integrals_in_polymer_science
Computer simulations to discover and understand chemical properties
protein structure by simulating folding of the polypeptide chain from a random coil. MD can also be used to compute other thermodynamic properties such as
Molecular_dynamics
Spectroscopy technique
indicates a variation in conformation of a polymer from spherical to random coil to linear. Combining the mean-square radius from MALS with the hydrodynamic
Multiangle_light_scattering
Geometric probability Hadwiger's theorem Integral geometry Random coil Stochastic geometry Vitale's random Brunn–Minkowski inequality Benford's law Pareto principle
Catalog of articles in probability theory
Catalog_of_articles_in_probability_theory
Extracellular matrix protein
(residues 25–1413) predicted by IUPred2A is 15.3%. A large proportion of random coil (73%) was predicted in SNED1 together with 26% of β-strands, and 1% of
SNED1
Technique to separate DNA or RNA fragments
matrix as a sieve consisting of randomly distributed network of inter-connected pores. A globular protein or a random coil DNA moves through the connected
Gel electrophoresis of nucleic acids
Gel_electrophoresis_of_nucleic_acids
existing proteins found in nature. This synthetic NE peptide adopts random coil conformation and showing strong immunogenicity (computational prediction)
NE-tag
Computational models of intrinsically-disordered proteins
extremely high, flexible/disordered protein generally differ from fully random coil structures. The main purpose of these models is to gain insights regarding
Conformational_ensembles
Protein-coding gene in humans
very little specific secondary structure composed of mostly random coil regions. Random coil regions constitute 75.00% of the protein, while alpha helices
KRABD3
"OnD-CRF: predicting order and disorder in proteins using conditional random fields". Bioinformatics. 24 (11): 1401–2. doi:10.1093/bioinformatics/btn132
List of disorder prediction software
List_of_disorder_prediction_software
dynamic structure so the noncatalytic region of RNase E would form a random coil, and each of these coils would act independently from the other ones.
Degradosome
as well as the two termini of the bound phospholipid move towards the random coil region (residue 36–44). >P. tomentosum phoratoxin A
Phoratoxin_and_viscotoxin
(the 3D folding of a polypeptide), secondary (alpha helices/beta sheets/random coils) and primary structure (linear amino acid sequences linked by peptide
Ancient_protein
Protein and gene in humans
structure composition shows that most of the secondary structure consists of random coils. No disulfide bonds are predicted to be present. Membrane topology of
TMEM128
Chemical compound
M), proteins lose their ordered structure, and they tend to become randomly coiled, i.e. they do not contain any residual structure. However, at concentrations
Guanidinium_chloride
Protein-coding gene in humans
The secondary structure of ALAESM is predicted to be structured as 55% random coil, 35% alpha helix and 9% extended strand. There are two alpha helices
C1orf122
Enzyme
NAD-BD. The antenna consists of an ascending helix and a descending random coil strand that contains a small α-helix toward the C-terminal end of the
Glutamate_dehydrogenase_1
Protein found in humans
presence of the Coiled-coil motif. The tertiary structure of CCDC121 is composed mostly of alpha helices and contains some random coil. Ali2D Secondary
CCDC121
Magnet that creates a magnetic field through an electric current
copper wire wound into a coil. A current through the wire creates a magnetic field which is concentrated along the center of the coil. The magnetic field disappears
Electromagnet
Process of evaluating 3-dimensional atomic models of biomacromolecules
several current or proposed methods for making this distinction such as Random Coil Index, but so far the NMR community has not standardized on one. Cyro-EM
Structure_validation
unresolved problem for the biomolecular NMR community. Chemical Shift Random Coil Index Chemical shift index Protein NMR RefDB (chemistry) SHIFTCOR Protein
Protein chemical shift re-referencing
Protein_chemical_shift_re-referencing
1995 studio album by ELpH vs. Coil
"ELpH vs. Coil", released in 1995, though an EP called Born Again Pagans is also credited to "Coil vs. ELpH". ELpH is the alias name that Coil used to describe
Worship_the_Glitch
transmembrane domain. It is also predicted that SMIM14 is randomly coiled near the C-terminus. A random coil is regarded as the protein's lack of a secondary structure
Small integral membrane protein 14
Small_integral_membrane_protein_14
Order of wingless insects
Sutherland, Tara D. (2013). "Silverfish silk is formed by entanglement of randomly coiled protein chains". Insect Biochemistry and Molecular Biology. 43 (7):
Archaeognatha
Protein-coding gene in the species Homo sapiens
Secondary structure of C21orf58 is predicted to consist primarily of random coil domains with four regions of alpha helices throughout the span of the
C21orf58
Protein-coding gene in the species Homo sapiens
nuclear protein. The secondary structure of RESF1 consists of mainly random coil structures (approximately 59.2%), few alpha helices (24% of residues)
RESF1
Solvent property in polymer science
θ solvent) is a solvent in which polymer coils act like ideal chains, assuming exactly their random walk coil dimensions.[clarification needed] Therefore
Theta_solvent
Protein found in humans
of CCDC42B is predicted to contain several alpha-helices, and other random coils. Hairpin loop structures were detected at the 5'UTR and 3'UTR region
CFAP73
accessible surface areas (a value ranging from 0 to 1.0). Exposed, exterior, random coil or hydrophilic residues typically have a large fractional accessible
Volume Area Dihedral Angle Reporter
Volume_Area_Dihedral_Angle_Reporter
Protein-coding gene in the species Homo sapiens
in α-helices with random coils in between. More precisely, the protein is predicted to be composed of 62.9% α-helix, 33.8% random coil, and 3.3% extended
SLC46A3
Human protein-encoding gene on chromosome 7
secondary structure composed of alpha helices, random coil regions and extended strands. Random coil regions are most found in c7orf26, as they constitute
INTS15
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