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  2. Adapter (genetics) - Wikipedia

    en.wikipedia.org/wiki/Adapter_(Genetics)

    NGS adapters are short ~80 BP fragments that bind to DNA to aid in amplification during library preparation and are also useful to bind DNA to the flow cell during sequencing. [5] These adapters are made up of three parts that flank the DNA sequence of interest. There is the flow cell binding sequence, the primer binding site, and also tagged ...

  3. Globin - Wikipedia

    en.wikipedia.org/wiki/Globin

    Myoglobin (Mb) Neuroglobin: a myoglobin-like haemprotein expressed in vertebrate brain and retina, where it is involved in neuroprotection from damage due to hypoxia or ischemia. [11] Neuroglobin belongs to a branch of the globin family that diverged early in evolution. Cytoglobin: an oxygen sensor expressed in multiple tissues. Related to ...

  4. Myoglobin - Wikipedia

    en.wikipedia.org/wiki/Myoglobin

    Like hemoglobin, myoglobin is a cytoplasmic protein that binds oxygen on a heme group. It harbors only one globulin group, whereas hemoglobin has four. Although its heme group is identical to those in Hb, Mb has a higher affinity for oxygen than does hemoglobin but fewer total oxygen-storage capacities. [22]

  5. Affinity chromatography - Wikipedia

    en.wikipedia.org/wiki/Affinity_chromatography

    For thoroughness, the GST protein and the GST-fusion protein can each be coupled separately. The serum is initially allowed to bind to the GST affinity matrix. This will remove antibodies against the GST part of the fusion protein. The serum is then separated from the solid support and allowed to bind to the GST-fusion protein matrix.

  6. Transition metal dioxygen complex - Wikipedia

    en.wikipedia.org/wiki/Transition_metal_dioxygen...

    Myoglobin and hemoglobin are famous examples, and many synthetic analogues have been described that behave similarly. Binding of O 2 is usually described as proceeding by electron transfer from the metal(II) center to give superoxide (O − 2) complexes of metal(III) centers.

  7. Cytoglobin - Wikipedia

    en.wikipedia.org/wiki/Cytoglobin

    Cytoglobin has 30-40% sequence homology with myoglobin, and has a similar oxygen binding affinity. One of the major differences is the presence of a 20 amino acids extension at both the n and c terminus. [11] Cytoglobin is a hexacoordinate heme protein.

  8. Cooperative binding - Wikipedia

    en.wikipedia.org/wiki/Cooperative_binding

    The first description of cooperative binding to a multi-site protein was developed by A.V. Hill. [4] Drawing on observations of oxygen binding to hemoglobin and the idea that cooperativity arose from the aggregation of hemoglobin molecules, each one binding one oxygen molecule, Hill suggested a phenomenological equation that has since been named after him:

  9. Sarcoplasm - Wikipedia

    en.wikipedia.org/wiki/Sarcoplasm

    Sarcoplasm is the cytoplasm of a muscle cell.It is comparable to the cytoplasm of other cells, but it contains unusually large amounts of glycogen (a polymer of glucose), myoglobin, a red-colored protein necessary for binding oxygen molecules that diffuse into muscle fibers, and mitochondria.

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