Cytoglobin: Difference between revisions

Line 12:

Cytoglobin is a 44.72 KDa protein, containing 190 amino acids<ref>https://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=2DC3</ref>. The structure of Cytoglobin is largely alpha helices. The structure also contains a folding pattern characteristic of other globin-like proteins. It contains 8 alpha helices in a 3-over-3 sandwich conformation. CATH classifies each chain of the protein as 1.10.490.103<ref>http://cathdb.info/version/latest/domain/2dc3A00</ref>.

The homodimer is stabilized by electrostatic interactions, hydrogen bonding, and an inter-subunit disulfide bridge at CYS38 and CYS832. The most highly conserved residues are the residues involved in the hydrophobic heme pocket, distal and proximal histidine residues, and the inter-subunit disulfide bridge. This is, once again, indicative of potential protein function<ref>https://link.springer.com/article/10.1007/s00018-011-0764-9</ref>. Studies using immunoprecipitation/mass spectrometry did not find any interacting partners of cytoglobin<ref>https://link.springer.com/article/10.1007/s00018-011-0764-9</ref>. Experiments conducted with high concentrations of CYGB have found that it was present only in the monomeric form<ref>https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4925767/</ref>.

The homodimer is stabilized by electrostatic interactions, hydrogen bonding, and an inter-subunit <scene name='74/748876/Disulfide/1'>disulfide bridge</scene> at CYS38 and CYS832. The most highly conserved residues are the residues involved in the hydrophobic heme pocket, distal and proximal histidine residues, and the inter-subunit disulfide bridge. This is, once again, indicative of potential protein function<ref>https://link.springer.com/article/10.1007/s00018-011-0764-9</ref>. Studies using immunoprecipitation/mass spectrometry did not find any interacting partners of cytoglobin<ref>https://link.springer.com/article/10.1007/s00018-011-0764-9</ref>. Experiments conducted with high concentrations of CYGB have found that it was present only in the monomeric form<ref>https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4925767/</ref>.

Cytoglobin: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

Revision as of 00:46, 28 April 2020 view source Dana M. Grass (talk \| contribs) 5 edits I worked on a project recently researching cytoglobin and I am uploading my findings to proteopedia. ← Older edit		Revision as of 00:57, 28 April 2020 view source Dana M. Grass (talk \| contribs) 5 edits No edit summary Newer edit →
Line 12:		Line 12:
	Cytoglobin is a 44.72 KDa protein, containing 190 amino acids<ref>https://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=2DC3</ref>. The structure of Cytoglobin is largely alpha helices. The structure also contains a folding pattern characteristic of other globin-like proteins. It contains 8 alpha helices in a 3-over-3 sandwich conformation. CATH classifies each chain of the protein as 1.10.490.103<ref>http://cathdb.info/version/latest/domain/2dc3A00</ref>.		Cytoglobin is a 44.72 KDa protein, containing 190 amino acids<ref>https://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=2DC3</ref>. The structure of Cytoglobin is largely alpha helices. The structure also contains a folding pattern characteristic of other globin-like proteins. It contains 8 alpha helices in a 3-over-3 sandwich conformation. CATH classifies each chain of the protein as 1.10.490.103<ref>http://cathdb.info/version/latest/domain/2dc3A00</ref>.

	The homodimer is stabilized by electrostatic interactions, hydrogen bonding, and an inter-subunit disulfide bridge at CYS38 and CYS832. The most highly conserved residues are the residues involved in the hydrophobic heme pocket, distal and proximal histidine residues, and the inter-subunit disulfide bridge. This is, once again, indicative of potential protein function<ref>https://link.springer.com/article/10.1007/s00018-011-0764-9</ref>. Studies using immunoprecipitation/mass spectrometry did not find any interacting partners of cytoglobin<ref>https://link.springer.com/article/10.1007/s00018-011-0764-9</ref>. Experiments conducted with high concentrations of CYGB have found that it was present only in the monomeric form<ref>https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4925767/</ref>.		The homodimer is stabilized by electrostatic interactions, hydrogen bonding, and an inter-subunit <scene name='74/748876/Disulfide/1'>disulfide bridge</scene> at CYS38 and CYS832. The most highly conserved residues are the residues involved in the hydrophobic heme pocket, distal and proximal histidine residues, and the inter-subunit disulfide bridge. This is, once again, indicative of potential protein function<ref>https://link.springer.com/article/10.1007/s00018-011-0764-9</ref>. Studies using immunoprecipitation/mass spectrometry did not find any interacting partners of cytoglobin<ref>https://link.springer.com/article/10.1007/s00018-011-0764-9</ref>. Experiments conducted with high concentrations of CYGB have found that it was present only in the monomeric form<ref>https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4925767/</ref>.