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globin

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globin
globin (ˈgləʊbɪn) [f. L. glob-us globe n. + -in.] (See quot.1877.) Now more widely: any of various colourless basic polypeptides that are the protein components of hæmoglobin, myoglobin, and related molecules (the non-protein part in each case being hæm).1877 Foster Physiol. ii. ii. 241 The proteid ... Oxford English Dictionary
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Globin
The globin fold is found in its namesake globin families as well as in phycocyanins. The globin fold The globin fold (cd01067) also includes some non-haem proteins. wikipedia.org
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HBB (disambiguation)
HBB could refer to: Science Hexabromobenzene Beta globin (HBB, β-globin or haemoglobin, beta) a globin protein in adult human hemoglobin A. Human β-globin locus Places Headbangers Ball National Rail station code for Hubberts Bridge railway station, England Television Has Bilgi Birikim wikipedia.org
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Hemoglobin subunit zeta
Zeta-globin is an alpha-like hemoglobin. The zeta-globin gene is a member of the human alpha-globin gene cluster that includes five functional genes and two pseudogenes. wikipedia.org
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What is the structural difference between beta and gamma globin chains of Hb? Hemoglobins are tetramers composed of pairs of two different polypeptide subunits. The subunit composition of the principal hemoglobins are...
Here's a pairwise sequence alignment of the human hemoglobin beta (HBB) and gamma (HBG1) chains: HBB_HUMAN 1 VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLST 50 .|.|.|:|:.:|:|||||||::.|||.|||||||||||||||:|||:||: HBG1_HUMAN 1 GHFTEEDKATITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGNLSS 50 HBB_HUMAN 51 PDAVMG...
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Hemoglobin A
Globin synthesis Globin synthesis takes place in the ribosomes which are located within the cytosol. 1 Alpha globin 2 Beta globin Delta globin References External links Hemoglobins wikipedia.org
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Pros and cons of amino acid structure vs DNA sequences for evolutionary comparison This is an analysis question for a lab on the amino acid differences in beta globin amongst different primates, and using such differe...
Amino acid (protein) structure has its advantages over raw DNA. Protein structure already has introns (noncoding regions) trimmed out which aren't obvious from a plain DNA string. A protein can have different shapes (such as unbound/bound) or even folded/misfolded (as in the case of prions). DNA doe...
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Locus control region
that was vital for expression of any of the β-globin genes. The β-globin LCR in mice and humans is found 6–22 kb upstream of the first globin gene (epsilon). wikipedia.org
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What is the reason for 'microcytic' anaemia? I know the causes for microcytic anaemia are Fe deficiency, prolonged inflammation, Thalessemia, Sideroblastic etc. All these logically point to a decrease in Haemoglobin s...
It can result from defects either in iron acquisition or availability, or in heme or globin synthesis.
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Human β-globin locus
This locus contains not only the beta globin gene but also delta, gamma-A, gamma-G, and epsilon globin. The order of the genes in the beta-globin cluster is: 5' - epsilon – gamma-G – gamma-A – delta – beta - 3'. wikipedia.org
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珠蛋白
珠蛋白都包含“珠蛋白折叠”（globin fold），此折叠为一串8个α螺旋的链段。 珠蛋白有两个重要的成员：肌红蛋白和血红蛋白，这两种蛋白质都借由血红素辅基可逆地与氧结合，且此两者广泛分布于许多生物体内。 wikipedia.org
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HBE1
Function The epsilon globin gene (HBE) is normally expressed in the embryonic yolk sac: two epsilon chains together with two zeta chains (an alpha-like globin) constitute the embryonic hemoglobin Hb Gower I; two epsilon chains together with two alpha chains form the embryonic Hb Gower II. wikipedia.org
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Hemoglobin subunit beta
Hemoglobin subunit beta (beta globin, β-globin, haemoglobin beta, hemoglobin beta) is a globin protein, coded for by the HBB gene, which along with alpha HbE has a very unstable α- and β-globin association. wikipedia.org
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HBG1
Function The gamma globin genes (HBG1 and HBG2) are normally expressed in the fetal liver, spleen and bone marrow. The order of the genes in the beta-globin cluster is: 5' - epsilon – gamma-G – gamma-A – delta – beta - 3'. wikipedia.org
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Hemoglobin H disease
The structure of Hb A consists of two α-globin chains bound to two β-globin chains to form a tetramer (a protein made up four protein chains). When there is lower than normal production of α-globin, as in Hb H disease, the excess β-globin form β4-tetramers, termed Hemoglobin H. wikipedia.org
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