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Secondary structure Sedimentation

Ribosomes, the supramolecular assemblies where protein synthesis occurs, are about 65% RNA of the ribosomal RNA type. Ribosomal RNA (rRNA) molecules fold into characteristic secondary structures as a consequence of intramolecular hydrogen bond interactions (marginal figure). The different species of rRNA are generally referred to according to their sedimentation coefficients (see the Appendix to Chapter 5), which are a rough measure of their relative size (Table 11.2 and Figure 11.25). [Pg.343]

Binding of heme by isolated N-domain causes a change in sedimentation coefficient consistent with a more compact conformation and leads to the more avid association with the C-domain (125). Sedimentation equilibrium analysis showed that the Kd decreases from 55 pM to 0.8 pM (Fig. 5) (106). In addition, the calorimetric AH (-1-11 kcal/mol) and AS (-1-65 kcal/mol K) for the heme-N-domain-C-domain interaction and the AH (-3.6 kcal/mol) and AS (-1-8.1 kcal/mol K) derived from van t Hoff analysis of ultracentrifuge data for the interaction in the absence of heme indicate that hydrophobic interactions predominate in the presence of heme and a mix (e.g., hydrophobic and van der Waals forces) drives the interaction in the absence of heme. However, FTIR spectra (Fig. 6) indicate that little change in the secondary structure of domains or intact hemopexin occurs upon heme binding (104). [Pg.215]

At pH 12, the disulfide and noncovalent bonds are both broken, and the monomer with a sedimentation constant of 1.45 Svedberg units is released. From frictional ratios, the monomer appears to exist as a coil with a diameter of 16 A and a length of 150 A. Analysis of the primary structure of K-casein (Loucheux-Lefebvre et al. 1978) suggests considerable secondary structure in the monomer. 23% a-helix, 31% /3-sheets, and 24% 0-turns. In contrast, other investigators, using several different approaches, obtained a-helix contents ranging from 0 to 20.8% (Bloomfield and Mead 1975). Circular dichroism spectra on the monomer indicated 14 and 31% for a-helix and / -sheet, respectively (Loucheux-Lefebvre et al 1978). An earlier study of the optical rotatory dispersion of the K-casein monomer yielded values for the a-helix content ranging from 2 to 16% (Herskovits 1966). [Pg.116]

Neothechnic developments Tectonic depression is apparent here filled with sea - continental sediments sunk in the Pliocene - quaternary layer to more than 1000 m Inter mountain depression filled with Pliocene quaternary continental sediments were sunk in the Pliocene -quaternary layer to more than 1000m. Mostly secondary and Paleogennic structures were lifted to more than 3000 min the neotechtonic period can be noted here. Mostly secondary and pre-secondary structures were lifted to more than 3000 m in die neotechtonic period. Mostly secondary and pre-secondary structures were lifted to more than 4000 m in the neotechtonic period. Continental fractions were sunk to more than2000m in the neotechtonic period. [Pg.253]

The mRNA transcript is a linear molecule but can have secondary structure through autocomplementarity as indicated above. In addition to mRNA there are other types of RNA, notably ribosomal RNA (rRNA) and transfer RNA (tRNA). The rRNAs in eukaryotes include 18S, 5.8S, 28S and 5S rRNAs (S, the Svedberg, being a measure of rate of sedimentation in ultracentrifugation and hence of relative size). The rRNAs have extensive secondary structure. The rRNAs and a number of proteins make up the ribosome upon which translation occurs. [Pg.77]

Relative to secondary structure, viscosity, sedimentation velocity, ultraviolet difference spectra and optical rotatory dispersion studies (4,24,25) showed that glutenin appears to be an assymetric molecule with a low a-helix content (10-15%). Glutenin contained more a-helix structure in hydrochloric acid solutions and less in urea solutions. The amount of a-helix structure is also influenced by changes in ionic strength (26). [Pg.198]

In eggs and ovaries of Xenopus laevis the three RNA species are present in a molar ratio of 1 1 (Dawid, 1972), and the G - - C content is 40, 43, and 44 (Dawid and Chase, 1972). More data on sedimentation coeflBcients and molecular weights are given in Tables X and XL Apparently because of pronounced changes in the secondary structure, the electrophoretic mobilities of the rRNA species are highly dependent on temperature and ionic strength of tbe medium as in a variety of animal cells (Mitra et ah, 1972 Dawid and Chase, 1972 and others). [Pg.417]

The clay fraction, which has long been considered as a very important and chemically active component of most solid surfaces (i.e., soil, sediment, and suspended matter) has both textural and mineral definitions [22]. In its textural definition, clay generally is the mineral fraction of the solids which is smaller than about 0.002 mm in diameter. The small size of clay particles imparts a large surface area for a given mass of material. This large surface area of the clay textural fraction in the solids defines its importance in processes involving interfacial phenomena such as sorption/desorption or surface catalysis [ 17,23]. In its mineral definition, clay is composed of secondary minerals such as layered silicates with various oxides. Layer silicates are perhaps the most important component of the clay mineral fraction. Figure 2 shows structural examples of the common clay solid phase minerals. [Pg.111]

All organisms synthesize carbohydrates, lipids, proteins, and polynucleotides, although the details of their molecular structures can be somewhat species specific. These basic classes of macromolecules have changed little over geologic time. The secondary metabolites are more species specific and have also changed little over geologic time. Many are resistant to degradation, and those provide excellent biomarkers that have been preserved in ancient marine sediments and petroleum deposits. [Pg.575]


See other pages where Secondary structure Sedimentation is mentioned: [Pg.193]    [Pg.13]    [Pg.53]    [Pg.102]    [Pg.103]    [Pg.67]    [Pg.385]    [Pg.74]    [Pg.296]    [Pg.321]    [Pg.385]    [Pg.314]    [Pg.447]    [Pg.17]    [Pg.471]    [Pg.79]    [Pg.126]    [Pg.644]    [Pg.206]    [Pg.390]    [Pg.41]    [Pg.179]    [Pg.209]    [Pg.469]    [Pg.606]    [Pg.29]    [Pg.572]    [Pg.574]    [Pg.340]   
See also in sourсe #XX -- [ Pg.10 ]




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