Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Wild greens

Turtle farming has been attempted in the Cayman Islands, but with little success for the hawksbill. There has been much more success with green turtles, but although the shell is thicker than that of wild green turtles, the material is not of very good quality and it tends to crack. It also has a high salt content, which makes it imsuitable for moulding. [Pg.139]

Triazine resistance found in one plant of the wild green foxtail was transferred to the cultivated foxtail millet to improve weed control in this crop (47). Growing foxtail millet with atrazine resistant cytoplasm in areas infested with green foxtail may result in the fertilization of some florets of cultivated spikes by pollen from wild plants. This is likely to occur close to the border of a field, where wild plants grow, as well as within a field where some plants survived herbicide applications. Spontaneous hybridizations lead to less than 0.01% hybrids of the crop (unpublished data), and nearly 0.2% of the wild plants (45). [Pg.361]

If you don t have room for more than a couple of herbs or leafy vegetables in your window boxes, you can still enjoy herby soups, dishes of spinachlike greens, and salads with a selection of tangy leaves by collecting wild greens. [Pg.60]

A tender wild green, with a taste like corn salad, that can be picked all year except when trosty. Add to salads. [Pg.62]

Also, the Phe-64 Leu and Ser-65 Thr mutant shows also higher fluorescence parameters comparative to the wild green fluorescent protein. Excitation at 458 nm yields a fluorescence spectrum with two peaks at 512 and 530 nm The fluorescence properties of this enhanced green fluorescent protein (EGFP) were found similar to the recombinant glutathione S-transferase-EGFP (GST-EGFP) protein, expressed in Escherichia coli (Cinelli et al. 2004). [Pg.221]

Rick CM (1974) High soluble solids content in large fruited tomato lines derived from a wild green fruited species. Hilgardia 42 493-510... [Pg.2879]

In rat models of acute inflammation and chronic arthritic inflammation, oral administration of extracts (alcohol and supercritical fluid) of wild, green celery seed suppressed NSAID-and ethanol-induced gastric injury, whereas against ibuprofen-induced gastrotoxicity, most commercial flavorant celery seed oils (derived from aged, brown seeds) were inactive. A similar outcome was found from celery seed products in a rat model of polyarthritis, some being effective anti-inflammatories (notably one made from wild, green seeds), whereas the majority were ineffective. ... [Pg.165]

Figure 17.4 Melting temperatures, Tm, of engineered single-, double-, and tripledisulfide-containing mutants of T4 lysozyme relative to wild-type lysozyme. The red bars show the differences in Tm values of the oxidized and reduced forms of the mutant lysozymes. The green bars for the multiple-bridged proteins correspond to the sum of the differences in Tm values for the constituent single-bridged lysozymes. (Adapted from M. Matsumura et al.. Nature 342 291-293, 1989.)... Figure 17.4 Melting temperatures, Tm, of engineered single-, double-, and tripledisulfide-containing mutants of T4 lysozyme relative to wild-type lysozyme. The red bars show the differences in Tm values of the oxidized and reduced forms of the mutant lysozymes. The green bars for the multiple-bridged proteins correspond to the sum of the differences in Tm values for the constituent single-bridged lysozymes. (Adapted from M. Matsumura et al.. Nature 342 291-293, 1989.)...
Figure 17.10 Construction of a two helix truncated Z domain, (a) Diagram of the three-helix bundle Z domain of protein A (blue) bound to the Fc fragment of IgG (green). The third helix stabilizes the two Fc-binding helices, (b) Three phage-display libraries of the truncated Z-domaln peptide were selected for binding to the Fc. First, four residues at the former helix 3 interface ("exoface") were sorted the consensus sequence from this library was used as the template for an "intrafece" library, in which residues between helices 1 and 2 were randomized. The most active sequence from this library was used as a template for five libraries in which residues on the Fc-binding face ("interface") were randomized. Colored residues were randomized blue residues were conserved as the wild-type amino acid while yellow residues reached a nonwild-type consensus, [(b) Adapted from A.C. Braisted and J.A. Wells,... Figure 17.10 Construction of a two helix truncated Z domain, (a) Diagram of the three-helix bundle Z domain of protein A (blue) bound to the Fc fragment of IgG (green). The third helix stabilizes the two Fc-binding helices, (b) Three phage-display libraries of the truncated Z-domaln peptide were selected for binding to the Fc. First, four residues at the former helix 3 interface ("exoface") were sorted the consensus sequence from this library was used as the template for an "intrafece" library, in which residues between helices 1 and 2 were randomized. The most active sequence from this library was used as a template for five libraries in which residues on the Fc-binding face ("interface") were randomized. Colored residues were randomized blue residues were conserved as the wild-type amino acid while yellow residues reached a nonwild-type consensus, [(b) Adapted from A.C. Braisted and J.A. Wells,...
Figure 17.14 Model of evolved mutant from cephalosphorinase shuffling. The sequence of the most active cephalosporinase mutant was modeled using the crystal structure of the class C cephalosporinase from Enterobacter cloacae. The mutant and wild-type proteins were 63% identical. This chimeric protein contained portions from three of the starting genes, including Enterobacter (blue), Klebsiella (yellow), and Citrobacter (green), as well as 33 point mutations (red). (Courtesy of A. Crameri.)... Figure 17.14 Model of evolved mutant from cephalosphorinase shuffling. The sequence of the most active cephalosporinase mutant was modeled using the crystal structure of the class C cephalosporinase from Enterobacter cloacae. The mutant and wild-type proteins were 63% identical. This chimeric protein contained portions from three of the starting genes, including Enterobacter (blue), Klebsiella (yellow), and Citrobacter (green), as well as 33 point mutations (red). (Courtesy of A. Crameri.)...
Tang Kou Bird Tongue Wild Bird Tongue Yue Xi Green Orchid... [Pg.83]

Gonczy This is very difficult to quantitate. As you have seen from the immunofluorescence images, there are many microtubules on either side in wild-type moreover, anaphase B takes places within a couple of minutes. Therefore, it will be difficult to uncover potential transient changes in microtubule numbers using fixed specimens. However, we have generated a green fluorescent protein... [Pg.178]

Bell AF, Stoner-Ma D, Wachter RM, Tonge PJ (2003) Light-driven decarboxylation of wild-type green fluorescent protein. J Am Chem Soc 125 6919-6926... [Pg.376]

Lossau H, Rummer A, Heinecke R, Pollinger-Dammer F, Kompa C, Bieser G, Jonsson T, Silva CM, Yang MM, Youvan DC, Michel-Beyerle ME (1996) Time-resolved spectroscopy of wild-type and mutant green fluorescent proteins reveals excited state deprotonation consistent with fluorophore-protein interactions. Chem Phys 213 1-16... [Pg.378]

Fig. 7.1 Mutation of Thr164 to lie (cyan) in the fourth transmembrane region of the / 2-adrener-gic receptor leads to steric interference with Ser165 (green) within the active site of the receptor. (A) general domain structure and position of the residues, (B) wild type, (C) mutant showing interaction of lie164 with Ser165. Fig. 7.1 Mutation of Thr164 to lie (cyan) in the fourth transmembrane region of the / 2-adrener-gic receptor leads to steric interference with Ser165 (green) within the active site of the receptor. (A) general domain structure and position of the residues, (B) wild type, (C) mutant showing interaction of lie164 with Ser165.

See other pages where Wild greens is mentioned: [Pg.260]    [Pg.16]    [Pg.60]    [Pg.62]    [Pg.1134]    [Pg.1135]    [Pg.260]    [Pg.16]    [Pg.60]    [Pg.62]    [Pg.1134]    [Pg.1135]    [Pg.29]    [Pg.313]    [Pg.335]    [Pg.399]    [Pg.1087]    [Pg.1090]    [Pg.1125]    [Pg.62]    [Pg.780]    [Pg.116]    [Pg.250]    [Pg.358]    [Pg.360]    [Pg.490]    [Pg.358]    [Pg.40]    [Pg.45]    [Pg.352]    [Pg.359]    [Pg.434]    [Pg.63]    [Pg.105]    [Pg.115]    [Pg.228]    [Pg.186]    [Pg.185]    [Pg.193]   


SEARCH



Wilde

© 2024 chempedia.info