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Residue Composition (residue + composition)
Selected AbstractsDust from comet Wild 2: Interpreting particle size, shape, structure, and composition from impact features on the Stardust aluminum foilsMETEORITICS & PLANETARY SCIENCE, Issue 1-2 2008A. T. Kearsley By comparison to laboratory shots of known particle dimensions and density, using the same velocity and incidence geometry as the Stardust Wild 2 encounter, we can derive size and mass of the cometary dust grains. Using scanning electron microscopy (SEM) of foil samples (both flown on the mission and impacted in the laboratory) we have recognized a range of impact feature shapes from which we interpret particle density and internal structure. We have documented composition of crater residues, including stoichiometric material in 3 of 7 larger craters, by energy dispersive X-ray microanalysis. Wild 2 dust grains include coarse (>10 ,m) mafic silicate grains, some dominated by a single mineral species of density around 3,4 g cm,3 (such as olivine). Other grains were porous, low-density aggregates from a few nanometers to 100 ,m, with an overall density that may be lower than 1 g cm,3, containing mixtures of silicates and sulfides and possibly both alkali-rich and mafic glass. The mineral assemblage is very similar to the most common species reported from aerogel tracks. In one large aggregate crater, the combined diverse residue composition is similar to CI chondrites. The foils are a unique collecting substrate, revealing that the most abundant Wild 2 dust grains were of sub-micrometer size and of complex internal structure. Impact residues in Stardust foil craters will be a valuable resource for future analyses of cometary dust. [source] Structure of Escherichia coli uridine phosphorylase at 2.0,ÅACTA CRYSTALLOGRAPHICA SECTION D, Issue 1 2003F. Temple Burling The 2.0,Å crystal structure has been determined for Escherichia coli uridine phosphorylase (UP), an essential enzyme in nucleotide biosynthesis that catalyzes the phosphorolytic cleavage of the C,N glycosidic bond of uridine to ribose-1-phosphate and uracil. The structure determination of two independent monomers in the asymmetric unit revealed the residue composition and atomic details of the apo configurations of each active site. The native hexameric UP enzyme was revealed by applying threefold crystallographic symmetry to the contents of the asymmetric unit. The 2.0,Å model reveals a closer structural relationship to other nucleotide phosphorylase enzymes than was previously appreciated. [source] Dissecting membrane protein architecture: An annotation of structural complexityBIOPOLYMERS, Issue 10 2009Jaime Arce Abstract ,-Helical membrane proteins exist in an anisotropic environment which strongly influences their folding, stability, and architecture, which is far more complex than a simple bundle of transmembrane helices, notably due to helix deformations, prosthetic groups and extramembrane structures. However, the role and the distribution of such heterogeneity in the supra molecular organization of membrane proteins remains poorly investigated. Using a nonredundant subset of ,-helical membrane proteins, we have annotated and analyze the statistics of several types of new elements such as incomplete helices, intramembrane loops, helical extensions of helical transmembrane domains, extracellular loops, and helices lying parallel to the membrane surface. The relevance of the annotation scheme was studied using residue composition, statistics, physical chemistry, and symmetry of their distribution in relation to the immediate membrane environment. Calculation of hydrophobicity using different scales show that different structural elements appear to have affinities coherent with their position in the membrane. Examination of the annotation scheme suggests that there is considerable information content in the amino acid compositions of the different elements suggesting that it might be useful for structural prediction. More importantly, the proposed annotation will help to decipher the complex hierarchy of interactions involved in membrane protein architecture. © 2009 Wiley Periodicals, Inc. Biopolymers 91: 815,829, 2009. This article was originally published online as an accepted preprint. The "Published Online" date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com [source] Characterization of Cell Wall Enzyme Activities, Pectin Composition, and Technological Criteria of Strawberry Cultivars (Fragaria×ananassa Duch)JOURNAL OF FOOD SCIENCE, Issue 4 2004G. Lefever ABSTRACT: The effects of physical characteristics and cell wall enzymatic activities of several strawberry culti-vars were investigated for possible industrial use. The enzymes study showed that the softest varieties had the highest pectin methylesterase (PME) and polygalacturonase (PG) activities. Differences in alcohol-insoluble pectin, water-soluble pectin, and parietal residue compositions were observed between Darsanga ("firm fruit") and Senga sengana ("soft fruit"). Finally, the study of pectin composition of Darsanga and Senga sengana indicated that the softest fruit had the highest water-soluble pectin content. The measurement of fruit PME activity permitted a preliminary screening of fruit maturity characteristics. [source] | ||||||||||