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Hemoglobin assembly

Quaternary structure the four separate chains Of hemoglobin assembled S3 into an oligomeric protein... [Pg.47]

Quaternary structure the tour separate chains of hemoglobin assembled into an oligomeric proteir ... [Pg.141]

Royer WEJ, Zhu H, Gorr T, Flores J, Knapp J. Allosteric hemoglobin assembly diversity and similarity. J. Biol. Chem. 2005 280 27477-27480. [Pg.690]

Griffith, W. R Kaltashov, I. A., Highly asymmetric interactions between globin chains during hemoglobin assembly revealed by electrospray ionization mass spectrometry. Biochemistry 2003, 42, (33), 10024-10033. [Pg.104]

Many protein molecules are composed of more than one subunit, where each subunit is a separate polypeptide chain and can form a stable folded structure by itself. The amino acid sequences can either be identical for each subunit (as in tobacco mosaic virus protein), or similar (as in the a and )3 chains of hemoglobin), or completely different (as in aspartate transcarbamylase). The assembly of many identical subunits provides a very efficient way of constructing... [Pg.241]

Takeoka S, Ohgushi T, Terase K, et al. Layer-controlled hemoglobin vesicles by interaction of hemoglobin with a phospholipid assembly. Langmuir 1996 12 1755. [Pg.85]

The smaiier 40 S subunit consists of one moiecuie of 18 S rRNA and 33 protein moie-cuies. The iarger 60 S subunit contains three types of rRNA with sedimentation coef cients of 5 S, 5.8 S, and 28 S and 47 proteins. In the presence of mRNA, the subunits assemble to form the complete ribosome, with a mass about 650 times larger than that of a hemoglobin molecule. [Pg.250]

Any polymerization reaction in which the product of each elongation step can itself also undergo further polymerization. When the same types of bonds and/or conformational states that are present in the reactant(s) are generated within product(s) during elongation, the process is referred to as isodesmic polymerization. Such is the case for the indefinite polymerization of actin, tubulin, hemoglobin S, and tobacco mosaic virus coat protein. See Nudeation Protein Polymerization Actin Assembly Kinetics Microtubule Assembly Kinetics Microtubule Assembly Kinetics... [Pg.361]

BIOCHEMICAL SELF-ASSEMBLY ACTIN ASSEMBLY KINETICS HEMOGLOBIN S POLYMERIZATION MICROTUBULE ASSEMBLY KINETICS BIOCONJUGATE BIOCONVERSION BIOLEACHING... [Pg.727]

MICROSCOPIC DIFFUSION CONTROL MACROSCOPIC DIFFUSION CONTROL MICROSCOPIC REVERSIBILITY CHEMICAL REACTION DETAILED BALANCING, RRINCIRLE OF CHEMICAL KINETICS MICROTUBULE ASSEMBLY KINETICS BIOCHEMICAL SELF-ASSEMBLY ACTIN ASSEMBLY KINETICS HEMOGLOBINS POLYMERIZATION... [Pg.762]

Metal coordination is another important bonding opportunity with respect to self-assembly. This is important in many natural molecules such as hemoglobin and chlorophyll, where the metal atom acts both as the site of activity and as a centralizing agent with respect to shape and thus acts as a nucleating agent for self-assembly. [Pg.507]

Queuing by the post office Building of an ant hill Numbering of book pages DNA duplex formation Oligomeric assembly of hemoglobin... [Pg.87]

There are many other spontaneous associations of biopolymers in nature - such as the assembly of hemoglobin from the two a -dimers, and the more complex protein assembly process illustrated in Figure 5.6. [Pg.91]

Dintzis, H.M. (1961) Assembly of the peptide chains of hemoglobin. Proc. Natl. Acad. Sci. USA 47, 247-261. [Pg.1078]

See other pages where Hemoglobin assembly is mentioned: [Pg.180]    [Pg.82]    [Pg.195]    [Pg.180]    [Pg.82]    [Pg.195]    [Pg.1148]    [Pg.200]    [Pg.40]    [Pg.40]    [Pg.1148]    [Pg.200]    [Pg.71]    [Pg.257]    [Pg.29]    [Pg.30]    [Pg.564]    [Pg.131]    [Pg.243]    [Pg.86]    [Pg.206]    [Pg.239]    [Pg.69]    [Pg.82]    [Pg.354]    [Pg.85]    [Pg.468]    [Pg.566]    [Pg.675]    [Pg.301]    [Pg.940]    [Pg.114]    [Pg.243]    [Pg.36]    [Pg.1155]    [Pg.200]    [Pg.521]    [Pg.166]   
See also in sourсe #XX -- [ Pg.227 ]



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