Proteins contribution

The chloroisocyanurates can be used in the bleaching of cotton, synthetics, and their blends they do, however, attack proteinaceous fibers, such as silk or wool, presumably via active chlorine reaction with the peptide (amide) linkage. However, the chloroisocyanurates can be used as shrink-proofing agents in wool finishing (131), (see Textiles Wool). The same action of chlorine upon proteins contributes to the effectiveness of chloroisocyanurates in automatic dishwashers. [Pg.422]

PD Swartz, T Ichiye. Protein contributions to redox potentials of iron-sulfur proteins An energy minimization study. Biophys J 73 2733-2741, 1997. [Pg.413]

Etemad-Moghadam B, Guo S, Kemphues KJ 1995 Asymmetrically distributed PAR-3 protein contributes to cell polarity and spindle alignment in early C. elegans embryos. Cell 83 743-752... [Pg.180]

A surprising finding is that for 16 of the 19 Trps, protein contributes a red shift to the steady state Stokes shift, a result that is statistically very improbable. The extreme bias toward red shifts for the protein contributions suggests that protein electric fields relative to the modest ground-state dipole of the Trp residue may be important in the evolution of the protein folds. [Pg.316]

Rao W, Dahlheimer JL, Bardgett ME, Snyder AZ, Finch RA, Sartorelli AC et al. Choroid plexus epithelial expression of MDR1 P glycoprotein and multidmg resistance-associated protein contribute to the blood-cerebrospinalfluid drug-permeability barrier. Proc Natl Acad Sci USA 1999 96(7) 3900-3905. [Pg.206]

Phenylalanine and tryptophan contain aromatic side chains that, like the aliphatic amino acids, are also relatively non-polar and hydrophobic (Figure 1.4). Phenylalanine is unreactive toward common derivatizing reagents, whereas the indolyl ring of tryptophan is quite reactive, if accessible. The presence of tryptophan in a protein contributes more to its total absorption at 275-280nm on a mole-per-mole basis than any other amino acid. The phenylalanine content, however, adds very little to the overall absorbance in this range. [Pg.6]

The DNA double helix is stabilized by hydrophobic interactions resulbng from the individual base pairs stacking on top of each other in the nonpolar interior of the double helix (Figs. 4-1 and 4-2). The hydrogen bonds, like the hydrogen bonds of proteins, contribute somewhat to the overall stability of the double helix but contribute greatly to the specificity for forming the correct base pairs. An incorrect base pair would not... [Pg.50]

Myelin basic protein. In PNS myelin, MBP varies from approximately 5% to 18% of total protein, in contrast to the CNS, where it is close to 30% [ 1 ]. In rodents, the same four 21,18.5,17 and 14kDa MBPs found in the CNS are present in the PNS. In adult rodents, the 14kDa MBP is the most prominent component and is termed Pr in the PNS nomenclature. The 18.5 kDa component is present and is often referred to as the P, protein in the nomenclature of peripheral myelin proteins. Another species-specific variation in human PNS is that the major basic protein is not the 18.5 kDa isoform that is most prominent in the CNS but rather a form of about 17 kDa. It appears that MBP does not play as critical a role in myelin structure in the PNS as it does in the CNS. For example, the shiverer mutant mouse, which expresses no MBP (Table 4-2), has a greatly reduced amount of CNS myelin, with no compaction of the major dense line. By contrast, shiverer PNS has essentially normal myelin,both in amount and structure, despite the absence of MBP. This CNS/PNS difference in the role of MBP is probably because the cytoplasmic domain of P0 has an important role in stabilizing the major dense line of PNS myelin. Animals doubly deficient for P0 and MBP have a more severe defect in compaction of the PNS major dense line than P0-null mice, which indicates that both proteins contribute to compaction of the cytoplasmic surfaces in PNS myelin [23],... [Pg.64]

Data are not available for protein production worldwide. However, an estimate of the protein contribution provided by sweet potatoes can be made if we assume a mean dry matter content of 28% and a mean protein content of 5%. Based on these assumptions, the sweet potato provides 1.92 million metric tons of protein worldwide. The yield of protein would be 134 kg/ha using worldwide yield values or 184 kg/ha using US production values. [Pg.238]

R. Pal, W. A. Petri, Jr., Y. Barenholz, and R. R. Wagner, Lipid and protein contributions to the membrane surface potential of vesicular stomatitits virus probed by a fluorescent pH indicator, 4-heptadecyl-7-hydroxycoumarin, Biochim. Biophys. Acta 729, 185-192 (1983). [Pg.271]

So far, biological Mossbauer spectroscopy is only sensitive to iron (or to be more precise to the Fe isotope) which rules out the use of this technique to directly probe the Ni site. Unfortunately, the iron site seems to remain always in a low-spin state making its identification by Mossbauer very difficult since it will be probably unresolved from the [3Fe-4S] and [4Fe-4S] cluster components. Also, each iron atom in the protein contributes equally to the Mossbauer spectrum the Fe site of the Ni-Fe centre is only 8.3 per cent of the total absorption. [Pg.154]

The ribosome is a unique cellular machine in that its main functional component is RNA whereas proteins seem to play only a structural role. For a long time, it has been debated whether RNA or proteins contribute most to the ribosome s function. With the determination of high-resolution crystal structures, this question could finally be answered. Clearly, these structures have revolutionized the field of ribosome studies. Already in the 1980s, Yonath and coworkers had grown crystals of active ribosomes that diffracted to about 0.6 nm (6 A) (1 A = 0.1nm) resolution. However, owing to the large size of the ribosome of about 2 500 000 Da (lDa=lgmoP), the ribosome structure was not solved to atomic resolution until tbe year 2000. [Pg.356]

Rao, V. V., Dahlheimer, J. L., Bardgett, M. E., et al. (1999) Choroid plexus epithelial expression of MDRl P glycoprotein and multidrug resistance-associated protein contribute to the blood-cerebrospinal-fluid drug-permeability barrier. Proc. Natl. Acad. Sci. U. S. A. 96, 3900-3905. [Pg.58]

Degradation of muscle protein contributes to weight loss and wasting in patients. It supplies aU amino acids for protein synthesis in tumour cells and some specific amino acids that have the following key roles ... [Pg.497]

Delmas P, Abogadie FC, Milligan G, Buckley NJ, Brown DA (1999) Py dimers derived from Go and Gj proteins contribute different components of adrenergic inhibiton of Ca channels in rat sympathetic neurons. J Physiol 518 23-36 Diverse-Pierluissi M, Inglese J, Stoffel RH, Lefkowitz RJ, Dunlap K (1996) G protein-coupled receptor kinase mediates desensitization of norepinephrine-induced Ca channel inhibition. Neuron 16 579-585 Docherty JR (1998) Subtypes of fimctional ap and a2-adrenoceptors. Eur J Pharmacol 361 1-15... [Pg.180]

Certain polypeptides resulting from protease digestion of proteins contribute to the typical taste of savoury foods. The DNA sequence coding for an octapep-tide known as beefy meaty peptide was cloned into yeast as a fusion with the yeast a factor to be secreted as free octapeptide into the medium which facilitated its recovery [37]. Alternatively, intracellular expression of tasty peptides... [Pg.517]

Kuehler and Stine (43) studied the functional properties of whey protein with respect to emulsifying capacity as affected by treatment with three proteolytic enzymes. Two microbial proteases and pepsin were examined. The emulsion capacity decreased as proteolysis continued, suggesting that there is an optimum mean molecular size of the whey proteins contributing to emulsification. [Pg.288]

Solubility and viscosity explains the basic physicochemical nature and the functional behavior of proteins in aqueous solutions. Proteins contribute to the adhesive or cohesive properties of film matrices by the binding of their polypeptides to other components such as starch granules to yield shaped products that, for example, are necessary for trapping gases in breadmaking. [Pg.339]

A review of how variations in structural stability within one protein contribute to function. [Pg.154]

Proteins are one of the most important ingredients in food production for both animals and humans. Besides having nutritional properties, protein contributes to the functional and organoleptic properties of food. The nutritional value of a protein depends on the total essential amino acid content. However, the availability of amino acids is conditioned by some protein attributes, mainly digestibility. [Pg.152]

Fig. 2. Evolution of the spectrin superfamily. Rounded rectangles represent spectrin repeats. Shaded rectangles denote a-actinin-like repeats involved in dimerization, whereas unshaded rectangles represent repeats that were involved in duplication and/ or elongation events. The incomplete spectrin repeats involved in tetramer formation are proportionally represented depending on the number of repeat helices each protein contributes to the formation of a complete spectrin repeat. (Adapted from Dubreuil, 1991 Pascual et al., 1997.) A dystrophin/utrophin ancestor probably diverged from a-actinin at a relatively early stage and then underwent its own series of duplications and acquisitions of new motifs.

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