sc321813 Search Results


human cygb protein  (OriGene)
90
OriGene human cygb protein
Fig. 7. Formation of disulfide bond between Cys38 and Cys83 induces the bending of the E helix and an increase of the distance between E and F helices. The figure shows the overlay of the hexa-coordinated crystal structure of the C38S/C83S mutant of <t>human</t> <t>Cygb</t> (purple, PDB ID: 1UT0) with a model of the penta-coordinated, ferric wild-type structure (cyan). The yellow dashed line indicates the distance between the alpha carbons of Ala88 (E helix) and Val105 (F helix). Molecular dynamics simulations indicate that the formation of the disulfide bond causes an increase in this interhelical distance (8.04 ± 0.64 Å vs 7.2 Å, respectively), allowing for the binding of hydrophobic chains in the hydrophobic core of Cygb.
Human Cygb Protein, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sc321813/Cytoglobin+(CYGB)+(NM_134268)+Human+Untagged+Clone/pm26928591-32-6-13
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human cygb protein - by Bioz Stars, 2026-09
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Fig. 7. Formation of disulfide bond between Cys38 and Cys83 induces the bending of the E helix and an increase of the distance between E and F helices. The figure shows the overlay of the hexa-coordinated crystal structure of the C38S/C83S mutant of human Cygb (purple, PDB ID: 1UT0) with a model of the penta-coordinated, ferric wild-type structure (cyan). The yellow dashed line indicates the distance between the alpha carbons of Ala88 (E helix) and Val105 (F helix). Molecular dynamics simulations indicate that the formation of the disulfide bond causes an increase in this interhelical distance (8.04 ± 0.64 Å vs 7.2 Å, respectively), allowing for the binding of hydrophobic chains in the hydrophobic core of Cygb.

Journal: Biochimica et biophysica acta

Article Title: Peroxidase activation of cytoglobin by anionic phospholipids: Mechanisms and consequences.

doi: 10.1016/j.bbalip.2016.02.022

Figure Lengend Snippet: Fig. 7. Formation of disulfide bond between Cys38 and Cys83 induces the bending of the E helix and an increase of the distance between E and F helices. The figure shows the overlay of the hexa-coordinated crystal structure of the C38S/C83S mutant of human Cygb (purple, PDB ID: 1UT0) with a model of the penta-coordinated, ferric wild-type structure (cyan). The yellow dashed line indicates the distance between the alpha carbons of Ala88 (E helix) and Val105 (F helix). Molecular dynamics simulations indicate that the formation of the disulfide bond causes an increase in this interhelical distance (8.04 ± 0.64 Å vs 7.2 Å, respectively), allowing for the binding of hydrophobic chains in the hydrophobic core of Cygb.

Article Snippet: In summary, the region encoding the human Cygb protein was cloned from the Origene (Rockville, MD) cDNA clone SC321813 (NM_134268) and inserted into the NcoI/HindIII restriction sites of the pET28a plasmid (Novagen) generating the pET28–HsaCygb plasmid.

Techniques: Mutagenesis, Binding Assay