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Implications of Neuroglobin Structure and Function in Human Brain Degenerative Disorders
Author(s) -
Demski Joshua Lee,
Beekman Ryley,
Ellcey Kaylee,
Guenzel Brandi,
Hollander Joshua,
Jodarski Alyssa,
Johnson Mckayla,
Moore Dillon
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.lb88
Subject(s) - neuroglobin , globin , oxygen transport , chemistry , function (biology) , oxygen , microbiology and biotechnology , neuroscience , biology , biochemistry , gene , organic chemistry
Neuroglobin is a respiratory protein with three possible ligands; oxygen, carbon dioxide, and a distal histidine of the protein itself. The unique structure of this protein allows for greater oxygen carrying potential in hypoxic or ischemic conditions. The Laconia High School MSOE Center for BioMolecular Modeling MAPS Team used 3‐D modeling and printing technology to examine structure‐function relationships of human neuroglobin. Internal cysteines at CD7 and D5 are close enough together to form a disulfide bond which has been shown to greatly increase oxygen affinity. Neuroglobin also has a hexacoordinated iron in its reduced state. The E7 His breaks its bond with iron when oxidized and allows for the transport of oxygen. The high expression levels of this globin point to many functions including a role in apoptosis, detoxification, signaling, and oxygen transport. Among this proteins many functions is a role in slowing neurodegenerative disorders by delaying apoptosis which when fully understood may provide treatment opportunities for neurodegenerative disorders such as Alzheimer's disease. While hundreds of studies on neuroglobin have been conducted its role in the human body is still poorly understood. Further research needs to be conducted to fully understand this highly conserved and doubtless crucial member of the globin family.