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  2. List of unsolved problems in biology - Wikipedia

    en.wikipedia.org/wiki/List_of_unsolved_problems...

    Unsolved problems relating to the structure and function of non-human organs, processes and biomolecules include: Korarchaeota (archaea). The metabolic processes of this phylum of archaea are so far unclear.

  3. Bioconcentration - Wikipedia

    en.wikipedia.org/wiki/Bioconcentration

    Fugacity and BCF relate to each other in the following equation: = [6] where Z Fish is equal to the Fugacity capacity of a chemical in the fish, P Fish is equal to the density of the fish (mass/length 3), BCF is the partition coefficient between the fish and the water (length 3 /mass) and H is equal to the Henry's law constant (Length 2 /Time 2) [6]

  4. List of partition topics - Wikipedia

    en.wikipedia.org/wiki/List_of_partition_topics

    Generally, a partition is a division of a whole into non-overlapping parts. Among the kinds of partitions considered in mathematics are partition of a set or an ordered partition of a set,

  5. Cell division - Wikipedia

    en.wikipedia.org/wiki/Cell_division

    [5] [6] After growth from the zygote to the adult, cell division by mitosis allows for continual construction and repair of the organism. [7] The human body experiences about 10 quadrillion cell divisions in a lifetime. [8] The primary concern of cell division is the maintenance of the original cell's genome.

  6. Plasmid partition system - Wikipedia

    en.wikipedia.org/wiki/Plasmid_partition_system

    The type III partition system is the most recently discovered partition system. It is composed of tubulin-like GTPase termed TubZ, and the CBP is termed TubR. Amino-acid sequence identity can go down to 21% for TubZ proteins. [7] The mechanism is similar to a treadmill mechanism: [24]

  7. Protein structure prediction - Wikipedia

    en.wikipedia.org/wiki/Protein_structure_prediction

    An alpha-helix with hydrogen bonds (yellow dots) The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns).

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