No description available.

Thesis (M.S.) in Chemical Engeneering--University of Maine, 2004. / Includes vita. Includes bibliographical references (leaves 97-99).

No description available.

Chloroplast and cytoplasmic ribosomes have been isolated from a number of species of the angiosperm genus Nicotiana. Ribosomal subunit and monosome proteins were separated by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). Resultant two-dimensional electrophoretic patterns of chloroplast and cytoplasmic ribosomal proteins were processed by a computer algorithm, developed to formally compare different electrophoretic patterns by the construction of two-dimensional, conformal average electrophoretic mobility maps. The chloroplast ribosomal subunit of N. tabacum contains 22-24 distinct basic polypeptides (pI > 5) and 2-3 acidic proteins (pI < 5). The 50S chloroplast ribosomal subunit possesses at least 1 acidic and 33-35 basic proteins. 40S and 60S cytoplasmic ribosomal subunits of the same species have 26-30 and 47-50 basic polypeptides, respectively. Molecular weights of chloroplast ribosomal proteins (ChRP) and cytoplasmic ribosomal proteins (CyRP) were estimated. There was little similarity between the 2D electrophoretic patterns of ChRP and CyRP of N. tabacum. However, 2D-PAGE patterns of N. tabacum ChRP and CyRP were qualitatively isomorphous with homologous patterns of Chlamydomonas reinhardi, pea and spinach. In terms of molecular weight and electrophoretic pattern N. tabacum ChRP were found to be more closely affiliated with prokaryotic ribosomal proteins than with CyRP from the same species. ChRP were isolated from N. gossei (an Australian species) and its reciprocol interspecies hybrids with N. tabacum (denoted by: T x G and G x T). Interspecies polymorphisms between homologous N. tabacum and N. gossei ChRP were delineated by computerized mobility mapping and co-electrophoresis of radiolabeled N. tabacum ChRP with a large molar excess of N. gossei ChRP. The inheritance mode (Mendelian vs. maternal) of a number of well-defined interspecies ChRP polymorphisms was determined by co-electrophoresis of radioiodinated N. tabacum ChRP with T x G and G x T hybrid ChRP. Results indicate that at least 4 30S ChRP and 3 50S ChRP are encoded by nuclear genes. 30S ChRP from an N. tabacum line carrying a maternally-inherited streptomycin-resistance mutation (SR-1) were compared to N. tabacum 30S ChRP by mobility mapping. Two differences were established between the SR-1 and wild-type 30S ChRP average mobility maps. These findings correlate with the reduced affinity of SR-1 30S chloroplast ribosomal subunits for ('3)H-dihydrostreptomycin, and show that at least one 30S ChRP is encoded by chloroplast DNA. Preparative 2D-PAGE and reverse high performance liquid chromatography (RPHPLC) separation techniques for complex ribosomal protein mixtures were developed. . . . (Author's abstract exceeds stipulated maximum length. Discontinued here with permission of author.) UMI

Li, Yuefang. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2010. / Includes bibliographical references (leaves 46-48). / Abstracts in English and Chinese. / Abstract --- p.i / 摘要 --- p.ii / Acknowledgement --- p.iii / Table of contents --- p.iv / Chapter Chapter 1 --- Introduction --- p.1 / Chapter 1.1 --- Introduction to protein crystallization --- p.1 / Chapter 1.1.1 --- Principles of protein crystallization --- p.2 / Chapter 1.1.2 --- Classical methods to crystallize protein --- p.4 / Chapter 1.2 --- Crystal growth in unique environments: the pursuit of better crystals --- p.6 / Chapter 1.2.1 --- Protein crystallization in space --- p.6 / Chapter 1.2.2 --- Crystallization in gel and capillary --- p.7 / Chapter 1.3 --- Microfluidic methods for protein crystallization: high through-put screenings --- p.9 / Chapter 1.3.1 --- Valve-controlled methods --- p.10 / Chapter 1.3.2 --- Droplet-based methods --- p.11 / Chapter 1.3.3 --- Microwell-based methods --- p.11 / Chapter 1.4 --- Objective of the project --- p.13 / Chapter Chapter 2 --- Rehydratable hydrogel in nanoliter microwells --- p.15 / Chapter 2.1 --- Introduction --- p.15 / Chapter 2.2 --- Experimental --- p.17 / Chapter 2.2.1 --- Fabrication of SU-8 mould --- p.17 / Chapter 2.2.2 --- Fabrication of the PDMS device --- p.19 / Chapter 2.2.3 --- Liquid dispensing in PDMS device --- p.20 / Chapter 2.2.4 --- Polymerization of PA gel --- p.21 / Chapter 2.2.5 --- Drying and Rehydration of PA gel --- p.22 / Chapter 2.3 --- Results and discussions --- p.23 / Chapter 2.3.1 --- Preparation of PA gel in PDMS device --- p.23 / Chapter 2.3.2 --- Immobilization of PA gel in microwells --- p.25 / Chapter 2.3.3 --- Dehydration and Rehydration of PA gel --- p.25 / Chapter 2.3.4 --- Liquid dispensing in the gel-preloaded microwells --- p.29 / Chapter 2.4 --- Conclusion --- p.31 / Chapter Chapter 3 --- Protein crystallization by gel-based FID --- p.32 / Chapter 3.1 --- Introduction --- p.32 / Chapter 3.2 --- Experimental --- p.34 / Chapter 3.2.1 --- Conditions used for crystallize proteins --- p.34 / Chapter 3.2.2 --- Protein crystallization by microbatch method --- p.34 / Chapter 3.2.3 --- Protein crystallization in microchip --- p.35 / Chapter 3.3 --- Results and discussions --- p.35 / Chapter 3.3.1 --- Crystallization in microplate --- p.36 / Chapter 3.3.2 --- Crystallization in microwells --- p.38 / Chapter 3.4 --- Conclusion --- p.41 / Chapter Chapter 4 --- Conclusions --- p.43 / Chapter 4.1 --- Summary of the work --- p.43 / Chapter 4.2 --- Future perspectives --- p.44 / Reference --- p.46

Not available / text

Metaproteomics, as a proteomic approach to analyse environmental samples, is a new and expanding field of research. The field promises new ways of determining the status of the organisms present in a sample, and could provide additional information compared to metagenomics. Being a novel field of research, robust methods and protocols have not yet been established. In this thesis, we examine several methods for a reliable extraction of protein from soil and periphyton samples. The extraction should preferably be fast, compatible with downstream analysis by mass spectrometry and extract proteins in proportion to their presence in the original sample. A variety of methods and buffers were used to extract proteins from soil and periphyton samples. Concentration determinations showed that all of these methods extracted enough protein for further analysis. For purification and digestion of the samples, several methods were used. The purified samples were analysed on three different mass spectrometers, with the Orbitrap Velos Pro delivering the best results. The results were matched against four genomic and metagenomic databases for identification of proteins, of which the UniProt/SwissProt database gave the best result. A maximum of 52 proteins were identified from periphyton samples when searching against UniProt/SwissProt with strict settings, of which the majority were highly conserved proteins. The main limitation for this type of work is currently the lack of proper metagenomic databases.

Thesis (M.S.)--Youngstown State University, 2008. / Includes bibliographical references (leaves 50-53). Also available via the World Wide Web in PDF format.

Thesis (Ph. D.)--University of Texas at Austin, 2003. / Supervisor: Adam Heller. Vita. Includes bibliographical references. Also available from UMI.

Fishes of the perciform suborder Notothenioidei are found in Antarctic and sub-Antarctic waters that are separated by the Antarctic Polar Front (APF), with some species being distributed on both sides of this front. In this wide latitudinal range, these fishes are exposed to different temperatures ranging from -2 °C in the High Antarctic regions to 12 °C in the sub-Antarctic regions. To survive in icy Antarctic waters, the Antarctic notothenioid species have evolved antifreeze glycoproteins (AFGPs) that prevent their body fluids from freezing. The findings of past research on the AFGP attributes of several notothenioid species inhabiting ice-free sub-Antarctic environments have presented a complex picture. Furthermore, previous taxonomic studies split widely distributed notothenioids into different species and/or subspecies, with other studies disagreeing with these splits. To understand the response of the sub-Antarctic notothenioids to warmer, ice-free environments, it is necessary to have a good understanding of their antifreeze biology and systematics. Therefore, this study aimed to determine the association, if any, between the antifreeze attributes of sub-Antarctic notothenioid fishes and their taxonomic status. And more...