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STRUCTURAL MOTIF

  • Structural motif
  • Type of common three-dimensional structure in chain-like biological molecules

    a structural motif is a common three-dimensional structure that appears in a variety of different, evolutionarily unrelated molecules. A structural motif

    Structural motif

    Structural_motif

  • Walker motifs
  • ATP-binding protein sequence motifs

    stays bound to the remaining phosphate groups. Walker motif A-binding has been shown to cause structural changes in the bound nucleotide, along the line of

    Walker motifs

    Walker_motifs

  • Motif (music)
  • Short recurring musical phrase

    composition. The motif is the smallest structural unit possessing thematic identity. The Encyclopédie de la Pléiade defines a motif as a "melodic, rhythmic

    Motif (music)

    Motif (music)

    Motif_(music)

  • Beta sheet
  • Protein structural motif

    The beta sheet (β-sheet, also β-pleated sheet) is a common motif of the regular protein secondary structure. Beta sheets consist of beta strands (β-strands)

    Beta sheet

    Beta sheet

    Beta_sheet

  • Leucine-rich repeat
  • Protein domain

    A leucine-rich repeat (LRR) is a protein structural motif that forms an α/β horseshoe fold. It is composed of repeating 20–30 amino acid stretches that

    Leucine-rich repeat

    Leucine-rich repeat

    Leucine-rich_repeat

  • Nucleic acid tertiary structure
  • Three-dimensional shape of a nucleic acid polymer

    easily recognizable tertiary structural motifs that serve as molecular building blocks. Some of the most common motifs for RNA and DNA tertiary structure

    Nucleic acid tertiary structure

    Nucleic acid tertiary structure

    Nucleic_acid_tertiary_structure

  • Inhibitor cystine knot
  • Protein structural motif

    Knottin) is a protein structural motif containing three disulfide bridges. Knottins are one of three folds in the cystine knot motif; the other closely related

    Inhibitor cystine knot

    Inhibitor cystine knot

    Inhibitor_cystine_knot

  • Cystine knot
  • Protein structural motif

    A cystine knot is a protein structural motif containing three disulfide bridges (formed from pairs of cysteine residues). The sections of polypeptide that

    Cystine knot

    Cystine knot

    Cystine_knot

  • Nest (protein structural motif)
  • The Nest is a type of protein structural motif. It is a small recurring anion-binding feature of both proteins and peptides.[excessive citations] Each

    Nest (protein structural motif)

    Nest (protein structural motif)

    Nest_(protein_structural_motif)

  • Helix-turn-helix
  • Structural motif capable of binding DNA

    The helix-turn-helix (HTH) is a major structural motif in proteins that functions as a DNA-binding domain (DBD). Each monomer incorporates two α helices

    Helix-turn-helix

    Helix-turn-helix

    Helix-turn-helix

  • Niche (protein structural motif)
  • In the area of protein structural motifs, niches are three or four amino acid residue features in which main-chain CO groups are bridged by positively

    Niche (protein structural motif)

    Niche (protein structural motif)

    Niche_(protein_structural_motif)

  • Rossmann fold
  • Protein fold

    conserved segment of the Rossmann fold. The motif is named after Michael Rossmann who first noticed this structural motif in the enzyme lactate dehydrogenase

    Rossmann fold

    Rossmann fold

    Rossmann_fold

  • Coiled coil
  • Structural motif in proteins

    A coiled coil is a structural motif in proteins in which two to seven alpha-helices are coiled together like the strands of a rope. (Dimers and trimers

    Coiled coil

    Coiled_coil

  • Motif (narrative)
  • Recurring element that has symbolic significance in a story

    such as the story's themes or mood. A narrative motif can be created through the use of imagery, structural components, language, and other elements throughout

    Motif (narrative)

    Motif_(narrative)

  • Sequence motif
  • Nucleotide or amino-acid sequence pattern

    encode the "structural motif" of a protein; that is a stereotypical element of the overall structure of the protein. Nevertheless, motifs need not be

    Sequence motif

    Sequence_motif

  • Beta bulge loop
  • Protein structural motif

    asparagine, serine or threonine at residue i, together with a nest (protein structural motif) at residues i+2 to i+4 (type 1) or residues i+3 to i+5 (type 2), with

    Beta bulge loop

    Beta bulge loop

    Beta_bulge_loop

  • Tetratricopeptide repeat
  • Protein domain

    The tetratricopeptide repeat (TPR) is a structural motif. It consists of a degenerate 34 amino acid tandem repeat identified in a wide variety of proteins

    Tetratricopeptide repeat

    Tetratricopeptide repeat

    Tetratricopeptide_repeat

  • Heptad repeat
  • The heptad repeat is an example of a structural motif that consists of a repeating pattern of seven amino acids: a b c d e f g H P P H C P C where H represents

    Heptad repeat

    Heptad_repeat

  • Omega loop
  • The omega loop is a non-regular protein structural motif, consisting of a loop of six or more amino acid residues and any amino acid sequence. The defining

    Omega loop

    Omega_loop

  • Alpha helix
  • Type of secondary structure of proteins

    binding motifs, including helix-turn-helix motifs, leucine zipper motifs and zinc finger motifs. This is because of the convenient structural fact that

    Alpha helix

    Alpha helix

    Alpha_helix

  • Supersecondary structure
  • Structural motif in proteins above the secondary structure level

    NAD within most dehydrogenases. Protein folding Secondary structure Structural motif "Helix Supersecondary Structures". biomedapps.curtin.edu.au. Retrieved

    Supersecondary structure

    Supersecondary_structure

  • Inhibitor of apoptosis domain
  • Protein domain

    repeat, Baculovirus Inhibitor of apoptosis protein Repeat, or BIR, is a structural motif found in proteins with roles in apoptosis, cytokine production, and

    Inhibitor of apoptosis domain

    Inhibitor of apoptosis domain

    Inhibitor_of_apoptosis_domain

  • Motif
  • Topics referred to by the same term

    in a protein Short linear motif, a stretch of protein sequence that mediates protein–protein interaction Structural motif, a pattern in a protein structure

    Motif

    Motif

  • Beta-sandwich
  • Two opposing antiparallel beta sheets that commonly occur in proteins

    Beta-sandwich or β-sandwich domains consisting of 80 to 350 amino acids occur commonly in proteins. They are characterized by two opposing antiparallel

    Beta-sandwich

    Beta-sandwich

    Beta-sandwich

  • Maltose
  • Chemical compound

    Maltose is the two-unit member of the amylose homologous series, the key structural motif of starch. When beta-amylase breaks down starch, it removes two glucose

    Maltose

    Maltose

    Maltose

  • Niche
  • Topics referred to by the same term

    describing the relational position of an organism's species Niche (protein structural motif) Stem-cell niche, the necessary cellular environment of a stem cell

    Niche

    Niche

  • Helix-hairpin-helix
  • Protein structural motif

    DNA-binding protein structural motif found in proteins that interact with DNA in a non-sequence-specific manner. The helix-hairpin-helix motif consists of two

    Helix-hairpin-helix

    Helix-hairpin-helix

    Helix-hairpin-helix

  • HbYX motifs
  • C-terminal position This structural arrangement is highly conserved across different species, from archaea to humans. The motif is found in various proteasome

    HbYX motifs

    HbYX motifs

    HbYX_motifs

  • Collagen helix
  • Main protein structure of fibrous collagen

    In molecular biology, the collagen triple helix or type-2 helix is the main secondary structure of various types of fibrous collagen, including type I

    Collagen helix

    Collagen helix

    Collagen_helix

  • Beta hairpin
  • Protein structural motif

    beta-beta unit) is a simple protein structural motif involving two beta strands that look like a hairpin. The motif consists of two strands that are adjacent

    Beta hairpin

    Beta hairpin

    Beta_hairpin

  • Transmembrane domain
  • Membrane-spanning protein domain

    A transmembrane domain (TMD, TM domain) is a membrane-spanning protein domain. TMDs may consist of one or several alpha-helices or a transmembrane beta

    Transmembrane domain

    Transmembrane_domain

  • Sterile alpha motif
  • Protein domain

    In molecular biology, the protein domain Sterile alpha motif (or SAM) is a putative protein interaction module present in a wide variety of proteins involved

    Sterile alpha motif

    Sterile alpha motif

    Sterile_alpha_motif

  • Zinc finger
  • Small structural protein motif found mostly in transcriptional proteins

    A zinc finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions (Zn2+) which stabilize the fold. The

    Zinc finger

    Zinc finger

    Zinc_finger

  • Schellman loop
  • Protein structural motif

    Schellman loops (also called Schellman motifs or paperclips) are commonly occurring structural features of proteins and polypeptides. Each has six amino

    Schellman loop

    Schellman loop

    Schellman_loop

  • Heptad
  • Topics referred to by the same term

    Heptad (computing), a group of 7 bits in computing Heptad repeat, a structural motif in proteins L'Heptade, an album by Harmonium in 1976 Sechtae, or "Heptads"

    Heptad

    Heptad

  • AspS RNA motif
  • Conserved RNA structure

    motif is a conserved RNA structure that was discovered by bioinformatics. aspS motifs are found in a specific lineage of Actinomycetota. aspS motif RNAs

    AspS RNA motif

    AspS RNA motif

    AspS_RNA_motif

  • Beta turn
  • Protein structural motif

    cause a change in direction of the polypeptide chain. They are very common motifs in proteins and polypeptides. Each consists of four amino acid residues

    Beta turn

    Beta_turn

  • Leucine zipper
  • DNA-binding structural motif

    leucine zipper (or leucine scissors) is a common three-dimensional structural motif in proteins. It was first described by Landschulz and collaborators

    Leucine zipper

    Leucine zipper

    Leucine_zipper

  • Basic helix–loop–helix
  • Protein structural motif

    A basic helix–loop–helix (bHLH) is a protein structural motif that characterizes one of the largest families of dimerizing transcription factors. The word

    Basic helix–loop–helix

    Basic helix–loop–helix

    Basic_helix–loop–helix

  • Non-canonical base pairing
  • Base pairs in molecular genetics

    different structural motifs, including pseudoknots, with their special hydrogen bonding features. Structural features of these recurrent motifs have been

    Non-canonical base pairing

    Non-canonical base pairing

    Non-canonical_base_pairing

  • Turn (biochemistry)
  • reverses its overall direction. According to one definition, a turn is a structural motif where the Cα atoms of two residues separated by a few (usually 1 to

    Turn (biochemistry)

    Turn_(biochemistry)

  • Polyproline helix
  • Type of protein secondary structure

    considered to be relatively rigid and used as a "molecular ruler" in structural biology, e.g., to calibrate FRET efficiency measurements. However, subsequent

    Polyproline helix

    Polyproline_helix

  • Allotropes of arsenic
  • black, or yellow allotropes. These various forms feature diverse structural motifs, with yellow arsenic enabling the widest range of reactivity. In particular

    Allotropes of arsenic

    Allotropes of arsenic

    Allotropes_of_arsenic

  • RING finger domain
  • Protein family

    New Gene) finger domain is a protein structural domain of zinc finger type which contains a C3HC4 amino acid motif which binds two zinc cations (seven

    RING finger domain

    RING finger domain

    RING_finger_domain

  • Tetraborate
  • alternate boron and oxygen atoms. Boroxole rings are a very common structural motif in polyborate ions. The hydrated tetraborate anion occurs in the mineral

    Tetraborate

    Tetraborate

    Tetraborate

  • Short linear motif
  • post-translational modifications that change the structural and physicochemical properties of the motif. Also, regions of high functional density can mediate

    Short linear motif

    Short linear motif

    Short_linear_motif

  • ATP-grasp
  • Protein structural motif

    molecular biology, the ATP-grasp fold is a unique ATP-binding protein structural motif made of two α+β subdomains that "grasp" a molecule of ATP between them

    ATP-grasp

    ATP-grasp

    ATP-grasp

  • Triple helix
  • Set of three congruent geometrical helices with the same axis

    making it an ideal protein for macromolecular transport and overall structural support throughout the body. There are some oligonucleotide sequences

    Triple helix

    Triple helix

    Triple_helix

  • Pi helix
  • Secondary protein structure

    LJ, Sondek J, Shortle D, Lattman EE (2000). "The alpha aneurism: a structural motif revealed in an insertion mutant of staphylococcal nuclease". Proc.

    Pi helix

    Pi helix

    Pi_helix

  • Structural alignment software
  • PMID 28065899. Bittrich S, Burley SK, Rose AS (2020). "Real-time structural motif searching in proteins using an inverted index strategy". PLOS Comput

    Structural alignment software

    Structural_alignment_software

  • PDZ domain
  • Protein family

    carboxylate group is bound by a nest (protein structural motif) in the PDZ domain, i.e. a PDZ-binding motif. PDZ is an acronym derived from the names of

    PDZ domain

    PDZ domain

    PDZ_domain

  • Aldol reaction
  • Chemical reaction

    These products are known as aldols, from the aldehyde + alcohol, a structural motif seen in many of the products. The use of aldehyde in the name comes

    Aldol reaction

    Aldol_reaction

  • Granin
  • Protein family

    proteins. Chromogranins and secretogranins together share a C-terminal motif, whereas chromogranins A and B share a region of high similarity in their

    Granin

    Granin

    Granin

  • Protein structure prediction
  • Type of biological prediction

    sequence motif databases are the Prosite catalog and the Stanford Motifs Database. Motif (structural context) a combination of several secondary structural elements

    Protein structure prediction

    Protein structure prediction

    Protein_structure_prediction

  • Thiadiazoles
  • Chemical compound

    possess no particular application, however, compounds bearing them as a structural motif are fairly common in pharmacology. Of them, 1,3,4-thiadiazole is the

    Thiadiazoles

    Thiadiazoles

  • Omega
  • Last letter of the Greek alphabet

    oxygen-18, a natural, stable isotope of oxygen. For omega loop, a protein structural motif consisting of a loop of six or more amino acid residues in any sequence

    Omega

    Omega

  • Ick
  • Topics referred to by the same term

    religious organization in Kosovo Inhibitor cystine knot, a protein structural motif Institute of Christ the King Sovereign Priest, a society of apostolic

    Ick

    Ick

  • GoLoco motif
  • Protein structural motif

    GoLoco motif is a protein structural motif. In heterotrimeric G-protein signalling, cell surface receptors (GPCRs) are coupled to membrane-associated

    GoLoco motif

    GoLoco motif

    GoLoco_motif

  • Histone fold
  • Protein family

    structural motif located near the C-terminus of histone proteins (H2/H3/H4), characterized by three alpha helices separated by two loops. This motif facilitates

    Histone fold

    Histone_fold

  • F-box protein
  • Protein containing at least one F-box domain

    targeted for degradation by the 26S proteasome. F-box domain is a protein structural motif of about 50 amino acids that mediates protein–protein interactions

    F-box protein

    F-box protein

    F-box_protein

  • WD40 repeat
  • Protein domain

    repeat (also known as the WD or beta-transducin repeat) is a short structural motif of approximately 40 amino acids, often terminating in a tryptophan-aspartic

    WD40 repeat

    WD40 repeat

    WD40_repeat

  • HKUST-1
  • Metal-organic framework material

    5-tricarboxylate linker molecules. The paddlewheel unit is the commonly used structural motif to describe the coordination environment of the metal centers and also

    HKUST-1

    HKUST-1

    HKUST-1

  • 310 helix
  • Type of secondary structure

    include the two most common structural motifs now known to occur. The following year, Linus Pauling predicted both of those motifs, the alpha helix and the

    310 helix

    310 helix

    310_helix

  • Nicotinamide adenine dinucleotide
  • Coenzyme

    One of the most common superfamilies includes a structural motif known as the Rossmann fold. The motif is named after Michael Rossmann, who was the first

    Nicotinamide adenine dinucleotide

    Nicotinamide adenine dinucleotide

    Nicotinamide_adenine_dinucleotide

  • Recognition sequence
  • DNA sequence (or subset thereof), to which the domain is specific

    A recognition sequence is a DNA sequence to which a structural motif of a DNA-binding domain exhibits binding specificity. Recognition sequences are palindromes

    Recognition sequence

    Recognition_sequence

  • Dockerin
  • Protein domain

    domain has two in-tandem repeats of a non-EF hand calcium binding motif. Each motif is characterized by a loop-helix structure. The three-dimensional

    Dockerin

    Dockerin

    Dockerin

  • EF hand
  • Protein helix–loop–helix motif

    hand is a helix–loop–helix structural domain or motif found in a large family of calcium-binding proteins. The EF-hand motif contains a helix–loop–helix

    EF hand

    EF hand

    EF_hand

  • Internal loop
  • Lehmann, J; Jossinet, F; Gautheret, D (May 1, 2013). "A universal RNA structural motif docking the elbow of tRNA in the ribosome, RNAse P and T-box leaders"

    Internal loop

    Internal_loop

  • Zwitterion
  • Molecule containing an equal number of positive and negative functional groups

    The compound trimethylglycine, named as "betaine", contain the same structural motif, a quaternary nitrogen atom with a carboxylate group attached to it

    Zwitterion

    Zwitterion

  • Ubiquitin ligase
  • Protein

    E3 ligase can in some cases also recognize structural motifs on the substrate. In this case, the 3D motif can allow the substrate to directly relate its

    Ubiquitin ligase

    Ubiquitin ligase

    Ubiquitin_ligase

  • Catgrip
  • Molecular binding feature

    Another tripeptide motif that often binds cations or δ+ groups via main chain CO groups is called the niche (protein structural motif). Watson, JD; Milner-White

    Catgrip

    Catgrip

    Catgrip

  • DNA-binding domain
  • Self-stabilizing region of a protein that binds to specific DNA sequences

    an independently folded protein domain that contains at least one structural motif that recognizes double- or single-stranded DNA. A DBD can recognize

    DNA-binding domain

    DNA-binding_domain

  • Fluorescein
  • Synthetic organic compound used as dye and fluorescent tracer

    Fluorescein is an organic compound and dye based on the xanthene tricyclic structural motif, formally belonging to triarylmethane dyes family. It is available

    Fluorescein

    Fluorescein

    Fluorescein

  • Gamma helix
  • Unobserved structure in protein

    on the amino acid's side chain (R) involved in this main-chain reversal motif, two stereoisomers can occur with their Cα-substituent located either in

    Gamma helix

    Gamma helix

    Gamma_helix

  • Dawson structure
  • Structural motif for heteropoly acids

    The Dawson structure is a well-known structural motif for heteropoly acids. The Dawson structure can be viewed as the fusion of two defect Keggin structure

    Dawson structure

    Dawson structure

    Dawson_structure

  • Alpha sheet
  • Secondary protein structure

    Implications for alpha-sheet as the possible amyloid intermediate. Journal of Structural Biology 213:α107738. Hilaire MR, Ding B, Mukherjee D, Chen J, Gai F. (2018)

    Alpha sheet

    Alpha sheet

    Alpha_sheet

  • Coiled coil (disambiguation)
  • Topics referred to by the same term

    Coiled coil may refer to: Coiled coil, a structural motif in proteins Coiled coil filament, a type of filament in incandescent light bulbs Coil (disambiguation)

    Coiled coil (disambiguation)

    Coiled_coil_(disambiguation)

  • PHD finger
  • Protein family

    a Cys4-His-Cys3 motif in the plant homeodomain (hence PHD) proteins HAT3.1 in Arabidopsis and maize ZmHox1a. The PHD zinc finger motif resembles the metal

    PHD finger

    PHD finger

    PHD_finger

  • OB-fold
  • Protein superfamily

    (oligonucleotide/oligosaccharide-binding fold) is a small protein structural motif observed in different proteins that bind oligonucleotides or oligosaccharides

    OB-fold

    OB-fold

    OB-fold

  • Protein secondary structure
  • General three-dimensional form of local segments of proteins

    folding Folding (chemistry) Nucleic acid secondary structure Translation Structural motif Protein circular dichroism data bank WHAT IF software List of protein

    Protein secondary structure

    Protein secondary structure

    Protein_secondary_structure

  • Type IX secretion system
  • in parallel with those of the type VI Secretion System (T6SS), sharing structural and energy-transducing similarities. Unlike injectisome-type systems,

    Type IX secretion system

    Type IX secretion system

    Type_IX_secretion_system

  • Structuralism
  • Intellectual current and methodological approach in the social science

    Structuralism is an intellectual current and methodological approach, primarily in the social sciences, that interprets elements of human culture by way

    Structuralism

    Structuralism

    Structuralism

  • TMPad
  • Repository of helix-helix interactions in membrane proteins

    Yi-Yuan; Sung Ting-Yi; Hsu Wen-Lian (Jan 2011). "TMPad: an integrated structural database for helix-packing folds in transmembrane proteins". Nucleic Acids

    TMPad

    TMPad

  • Amide ring
  • Small motifs in proteins and polypeptides

    Amide rings are small motifs in proteins and polypeptides. They consist of 9-atom or 11-atom rings formed by two CO...HN hydrogen bonds between a side

    Amide ring

    Amide_ring

  • ST turn
  • The ST turn is a structural feature in proteins and polypeptides. Each consists of three amino acid residues (labeled i, i + 1 and i + 2) in which residue

    ST turn

    ST turn

    ST_turn

  • ST motif
  • protein kinases. Structural studies of polypeptides indicate that such tetrapeptides can adopt the hydrogen bonding pattern of the ST motif. Wan, WY; Milner-White

    ST motif

    ST motif

    ST_motif

  • Beta bend ribbon
  • The beta bend ribbon, or beta-bend ribbon, is a structural feature in polypeptides and proteins. The shortest possible has six amino acid residues (numbered

    Beta bend ribbon

    Beta bend ribbon

    Beta_bend_ribbon

  • Pseudouridine
  • Chemical compound

    ubiquitous in this class of RNAs and facilitates common tRNA structural motifs. One such structural motif is the TΨC stem loop which incorporates Ψ55. Ψ is commonly

    Pseudouridine

    Pseudouridine

    Pseudouridine

  • Globular protein
  • Spherical, water-soluble type of protein

    hundreds of thousands of proteins and more elegant and descriptive structural motif vocabulary. The globular nature of these proteins can be determined

    Globular protein

    Globular protein

    Globular_protein

  • RAGE (receptor)
  • Protein-coding gene in the species Homo sapiens

    immunity and its ability to detect a class of ligands through a common structural motif, RAGE is often referred to as a pattern recognition receptor. RAGE

    RAGE (receptor)

    RAGE (receptor)

    RAGE_(receptor)

  • Structural biology
  • Study of molecular structures in biology

    structure Quaternary structure Structural domain Structural motif Protein subunit Molecular model Cooperativity Chaperonin Structural genomics Stereochemistry

    Structural biology

    Structural biology

    Structural_biology

  • Spiroketals
  • Heterocyclic Structure in Organic Chemistry

    spiroketals are structural motifs composed of two heterocycles sharing one central carbon which makes them a subclass of spiro compound. Their structural specificity

    Spiroketals

    Spiroketals

    Spiroketals

  • Phospholipid
  • Class of lipids

    and with the tails directed into the membrane. That is the dominant structural motif of the membranes of all cells and of some other biological structures

    Phospholipid

    Phospholipid

    Phospholipid

  • BNR/Asp-box repeat
  • Protein family

    PMID 8234325. Quistgaard EM, Thirup SS (July 2009). "Sequence and structural analysis of the Asp-box motif and Asp-box beta-propellers; a widespread propeller-type

    BNR/Asp-box repeat

    BNR/Asp-box repeat

    BNR/Asp-box_repeat

  • Asx turn
  • Feature in proteins and polypeptides

    The Asx turn is a structural feature in proteins and polypeptides. It consists of three amino acid residues (labeled i, i+1 and i+2) in which residue i

    Asx turn

    Asx_turn

  • HEAT repeat
  • Protein domain

    A HEAT repeat is a protein tandem repeat structural motif composed of two alpha helices linked by a short loop. HEAT repeats can form alpha solenoids,

    HEAT repeat

    HEAT repeat

    HEAT_repeat

  • Iron–sulfur protein
  • Proteins containing iron-sulfur clusters

    is a crucial step in the energy harvesting for many organisms. A common motif features a four iron ions and four sulfide ions placed at the vertices of

    Iron–sulfur protein

    Iron–sulfur_protein

  • Rutile
  • Oxide mineral composed of titanium dioxide

    CrO2. ZrO2 and HfO2 adopt another classical structural motif, the fluorite structure. In the rutile motif, the metal "cations" have a coordination number

    Rutile

    Rutile

    Rutile

  • Autochaperone
  • removed] Adhesion mediated by autotransporters of Gram-negative bacteria: Structural and functional features [2] Identification of Secretion Determinants of

    Autochaperone

    Autochaperone

  • Ribonucleoprotein particle
  • Protein complex

    processing of RNA transcripts. RBPs interact with RNA through various structural motifs. Aromatic amino acid residues in RNA-binding proteins result in stacking

    Ribonucleoprotein particle

    Ribonucleoprotein particle

    Ribonucleoprotein_particle

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