Top 10 similar words or synonyms for dodecamer

decamer    0.838139

heptamer    0.810056

heptamers    0.794152

undecamer    0.790550

dodecamers    0.773561

octamers    0.767807

octameric    0.748670

protomer    0.744641

hexadecamer    0.738025

nonamer    0.731894

Top 30 analogous words or synonyms for dodecamer

Article Example
Dodecameric protein A dodecamer (protein) is a protein complex with 12 protein subunits.
RuvB-like 1 RuvB-like 1 (E. coli), also known as RUVBL1 and TIP49, is a human gene. RUVBL1 can form a hexamer. The hexamer can form a dodecamer with RUVBL2 protein.
Group III pyridoxal-dependent decarboxylases The N-terminal domain has a flavodoxin-like fold, and is termed the "wing" domain because of its position in the overall 3D structure. Ornithine decarboxylase from "Lactobacillus" 30a (L30a OrnDC) is representative of the large, pyridoxal-5'-phosphate-dependent decarboxylases that act on lysine, arginine or ornithine. The crystal structure of the L30a OrnDC has been solved to 3.0 A resolution. Six dimers related by C6 symmetry compose the enzymatically active dodecamer (approximately 10 Da). Each monomer of L30a OrnDC can be described in terms of five sequential folding domains. The amino-terminal domain, residues 1 to 107, consists of a five-stranded beta-sheet termed the "wing" domain. Two wing domains of each dimer project inward towards the centre of the dodecamer and contribute to dodecamer stabilisation.
Polyphenol oxidase PPO is listed as a morpheein, a protein that can form two or more different homo-oligomers (morpheein forms), but must come apart and change shape to convert between forms. It exists as a monomer, trimer, tetramer, octamer or dodecamer, creating multiple (protein moonlighting functions. Substrate binding/turnover impacts multimerization, Different assemblies have different activities, Kinetic hysteresis).
Large tumor antigen The zinc-binding and ATPase domains together comprise the helicase portion of the LTag protein. The primary function of the zinc-binding domain is oligomerization of LTag. Formation of dodecamer structures (two hexameric rings) is required for helicase activity, which begins at the origin of replication through coordination between the OBD, zinc-binding, and ATPase domains.