Sökning: "Maria Selmer"
Visar resultat 6 - 10 av 10 avhandlingar innehållade orden Maria Selmer.
6. Antibiotic Resistance and the Cellular Currency S-adenosyl-methionine : Modification of aminoglycosides and nucleic acids
Sammanfattning : Streptomycin and spectinomycin are antibiotics that bind to ribosomes and inhibit protein synthesis. Common resistance mechanisms involve enzymatic modification of the two drugs by aminoglycoside nucleotidyltransferases (ANTs). The first part of this thesis covers the structural mechanism of two ANT enzymes. LÄS MER
7. Structural studies of small viruses using an X-ray Free Electron Laser
Sammanfattning : X-ray crystallography has since its introduction been the most successful technique for solving protein structures. Viruses however, often possess structural components such as fibrils, tails and envelopes that make them difficult or impossible to crystallize. LÄS MER
8. Structural and functional studies of streptococcal surface adhesins
Sammanfattning : The oral cavity is home to an array of microorganisms that are associated with dental plaque. Some Gram-positive bacteria are common inhabitants of the oral cavity and in order to colonize such a unique environment adhesion becomes essential and is accomplish by adhesins expressed on the bacterial surface. LÄS MER
9. Ribosomal RNA Modification Enzymes : Structural and functional studies of two methyltransferases for 23S rRNA modification in Escherichia coli
Sammanfattning : Escherichia coli ribosomal RNA (rRNA) is post-transcriptionally modified by site-specific enzymes. The role of most modifications is not known and little is known about how these enzymes recognize their target substrates. LÄS MER
10. The Importance of Being Promiscuous : Understanding enzyme function, specificity, and evolution through structure
Sammanfattning : Enzymes are known to be amazingly specific and efficient catalysts. However, many enzymes also have so-called promiscuous functions, i.e., they are able to catalyze other reactions than their main one. LÄS MER