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Showing 1 to 20 of 62 for “"Aminoacyl-tRNA"”.
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The Hydroxamate Reaction of Aminoacyl-tRNA Synthetases
<p>Amino acids are activated as aminoacyladenylates which remain bound to the aminoacyl-tRNA synthetases that catalyze their formation. The activated amino acids are then esterified to specific transfer RNA molecules. By this reaction sequence, the specificity and energetics necessary for …
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Modelling neuronal mitochondrial aminoacyl-tRNA synthetase defects
… and skeletal muscle. Mutations in mitochondrial aminoacyl-tRNA synthetase (MT-ARS) genes, which are crucial for mitochondrial protein synthesis and energy production via oxidative phosphorylation, are implicated in a variety of severe neurological and multisystemic diseases. Among these, …
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Functional analysis of a class II aminoacyl-tRNA synthetase
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1994.
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Experimental and Computational Dynamics of an Aminoacyl-tRNA Synthetase System
… is dependent upon correct recognition and aminoacylation of transfer RNA (tRNA) by their cognate aminoacyl-tRNA synthetases (AARSs). Methionine is the amino acid that acts as the start codon for every protein and can also be found within a protein message. Methionyl-tRNA synthetase (MetRS) …
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Investigations of peptide aminoacyl tRNA ligase (PEARL) biosynthetic gene clusters
Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2024-12-01
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Interactions Between Aminoacyl-Trna Synthetases and Transfer-Rnas From Escherichia Coli
Made available in DSpace on 2014-12-09T18:53:06Z (GMT). No. of bitstreams: 1 6901483.pdf: 1925547 bytes, checksum: 1341f16b04a547adb4610578659ace00 (MD5) Previous issue date: 1968
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NMR studies of RNA binding domains of human lysyl aminoacyl tRNA synthetase
<p>Human lysyl aminoacyl tRNA synthetase (hLysRS) is a multi-functional aminoacyl tRNA synthetase which is primarily involved in protein biosynthesis as well as crucial processes ranging from proinflammatory response to signal transduction. One important, non-canonical function of hLysRS is to …
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Characterizing the landscape of aminoacyl-tRNA synthetase protein production in Bacillus subtilis
… all cases. Here I use a model enzyme family, the aminoacyl tRNA synthetases (aaRS), to explore how sensitive Bacillus subtilis are to changes in aaRS production from the molecular to phenotypic level. This culmination of protein levels, functional output, and fitness, leads to a complete "fitness …
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Regulated alternative splicing separates canonical and cell signaling functions of aminoacyl-tRNA synthetases
Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2024-05-01
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Identification and Evolution of New Orthogonal Aminoacyl-tRNA Synthetase/tRNA Pairs for Genetic Code Expansion
… amino acids is the scalable discovery of aminoacyl-tRNA synthetase (aaRS)–tRNA pairs (the components of the cellular translational machinery which specify the matching between codons and amino acids) that are orthogonal in their aminoacylation specificity. An orthogonal pair is composed of …
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Localization of tRNAs and aminoacyl-tRNA synthetases in cytoplasm, chloroplast and mitochondria of Glycine max, L.
Dept. of Biological Sciences. Paper copy at Leddy Library: Theses & Major Papers - Basement, West Bldg. / Call Number: Thesis1980 .S553. Source: Masters Abstracts International, Volume: 40-07, page: . Thesis (M.Sc.)--University of Windsor (Canada), 1981.
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Investigating and expanding the functionality of RNA catalysts: Studies of the hepatitis delta virus, the hammerhead, and the aminoacyl-tRNA synthetase-like ribozymes
… ribozyme that mimics the function of the natural aminoacyl-tRNA synthetase. The design was based on the sequence of a naturally occurring riboswitch and an in vitro selected ribozyme that could charge tRNA with chemically synthesized unnatural amino acid substrates. The engineered ribozyme …
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FUNCTIONAL EFFECT OF ALTERATIONS TO E. coli METHIONYL-tRNA SYNTHETASE BETA-LINKER LENGTH
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that catalyze the
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Evolution of Protein Structure
The aminoacyl-tRNA synthetases are one of the major protein components in the translation machinery. These essential proteins are found in all forms of life, and are responsible for charging their cognate tRNAs with the correct amino acid. The evolution of the tRNA synthetases is of fundamental …
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Evaluation of the Protein Recognition Properties of Peptide Nucleic Acids
<p>The objective is to evaluate the ability of aminoacyl-tRNA synthetases (aaRS) to recognize the non-standard nucleic acid, PNA (peptide nucleic acid). PNA has immense potential in biomedical applications due to its increased thermostability and nuclease resistance over natural nucleic acids. PNA …
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Kinetic and mutational studies of two RNA-interacting enzymes
… which disrupt RNA secondary structure, and aminoacyl-tRNA synthetases, which catalyze the attachment of an amino acid to its cognate tRNA.
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BIOCHEMICAL ANALYSIS OF TWO DISTINCT METHIONYL-TRNA SYNTHETASES
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that catalyze the attachment of amino acids to their cognate tRNAs for protein biosynthesis at the ribosome. The long term objective of this project is to investigate catalytic features of methionyl-tRNA synthetase (MetRS) from two different …
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Characterization of Molecular Structure-Function Relationships of Escherichia Coli Leucyl-Trna Synthetase
The accurate covalent linkage of amino acid to tRNA for protein synthesis is catalyzed by a family of aminoacyl-tRNA synthetases (aaRS). Some aaRSs have the potential to make mistakes during aminoacylation due to the nature of their amino acid substrate. However, the synthetases have …
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Characterizing CMT-causing variants in tryptophanyl- tRNA synthetase
Aminoacyl-tRNA synthetases (aaRSs) are essential enzymes that link amino acids to their cognate tRNAs. Neurological conditions, such as Charcot-Marie-Tooth (CMT) disease, have been linked to variants identified in these enzymes. I created a humanized yeast model to assess the underlying …
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