Protein globins

Perhaps the most important complex of iron(II) is heme (or haeme). Haemoglobin, the iron-containing constituent of the blood, consists essentially of a protein, globin, attached through a nitrogen atom at one coordination position of an octahedral complex of iron(II). Of the other five coordination positions, four (in a plane) are occupied by nitrogen atoms, each of which is part of an organic... 

Having built a hidden Markov model for a particular family of proteins, it can then b< used to search a database. A score is computed for each sequence in the database anc those sequences that score significantly more than other sequences of a similar length ar( identified. This was demonstrated for two key families of proteins, globins and kinases ii the original paper [Krogh et al. 1994]. For the kinases, 296 sequences with a Z score abov<... 

Hemoglobin (Hb) is a conjugated protein the pro.sthetic group heme (hematin) and the protein (globin). which is composed of four polypeptide chain.s. are usually in identical pairs. The total M, is about 66.000. including four heme molecules. The molecule has an axis of. symmetry and. therefore. is composed of identical halves with an overall ellipsoid shape of the dimensions SS X S5 X 70 A. 

D. Although heme is contained in the cytochromes of the electron transport chain, the protein globin is not present. 

Oxygen transport in animals is performed by related pigments such as haem (Fig. 2.28), which is associated with a protein, globin, in haemoglobin.The metal atom in haems (iron) and chlorophylls (magnesium) is impor-... 

Hemoglobin is the respiratory protein for the red blood cells, and contains about 94% protein (globin) and 6% heme, which has the molecular formula C34H32FeN404-Each molecule combines with one molecule of oxygen to form oxyhemoglobin. 

Heme also regulates the synthesis of hemoglobin by stimulating synthesis of the protein globin. Heme maintains the ribosomal initiation complex for globin synthesis in an active state (see Chapter 15). 

Haemoglobin is an iron(II) complex of haem with the imidazole ring of the amino acid histidine contained in the protein globin. 

Miller and coworkers studied the energy flow between the protein and solvent using transient phase grating spectroscopy, which can monitor the temperature of the solvent matrix [39]. They demonstrated that energy transfer to the surrounding solvent occurred within 20 ps mediated by the protein backbone. A nanosecond time-scale was also observed, which was attributed to the slow conformational relaxation of the protein globin [40]. 

Since also this "a priori" statement is verified by the Fortran code analysis, it is by no means possible at present to conclude that the complementary strand gene distribution is statistically different from the coding strand gene distribution. Also the fact that the complementary distribution seems not to reach a peak at 140 < L < 150 codons cannot be applied in order to demonstrate a meaningful difference since, as we said previously, 5 out of the 17 genes analysed code for proteins (globin) of very close amino acid number. 

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