Change search
Refine search result
1 - 3 of 3
CiteExportLink to result list
Permanent link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Rows per page
  • 5
  • 10
  • 20
  • 50
  • 100
  • 250
Sort
  • Standard (Relevance)
  • Author A-Ö
  • Author Ö-A
  • Title A-Ö
  • Title Ö-A
  • Publication type A-Ö
  • Publication type Ö-A
  • Issued (Oldest first)
  • Issued (Newest first)
  • Created (Oldest first)
  • Created (Newest first)
  • Last updated (Oldest first)
  • Last updated (Newest first)
  • Disputation date (earliest first)
  • Disputation date (latest first)
  • Standard (Relevance)
  • Author A-Ö
  • Author Ö-A
  • Title A-Ö
  • Title Ö-A
  • Publication type A-Ö
  • Publication type Ö-A
  • Issued (Oldest first)
  • Issued (Newest first)
  • Created (Oldest first)
  • Created (Newest first)
  • Last updated (Oldest first)
  • Last updated (Newest first)
  • Disputation date (earliest first)
  • Disputation date (latest first)
Select
The maximal number of hits you can export is 250. When you want to export more records please use the Create feeds function.
  • 1.
    Almqvist, Jonas
    Stockholm University, Faculty of Science, Department of Physical, Inorganic and Structural Chemistry.
    Structural modeling of membrane transporter proteins2008Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    A fundamental process of all living organisms - the transport of molecules across cellular membranes through membrane transport proteins - is investigated.

    After a brief review of general properties of biological membranes follows a recollection of the major methods of membrane transport that Nature utilizes (Chapter 1). This is followed by a description of important experimental (Chapter 2) and theoretical methods (Chapter 3) for structural studies of membrane proteins. The findings on membrane protein transport in papers I-IV are then summarized (Chapter 4) and important findings are discussed. The remaining text is a discussion on relevant theoretical and experimental methods.

  • 2.
    Ericsson, Ulrika
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    A structural genomics pilot project: methods and applications2006Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    With the availability of many completely sequenced genomes, scientific research has shifted from genes to the products of the genes, the proteins. Structural genomics groups have been established worldwide, with the objective of determining protein structures on a genome-wide scale. New methods for protein production and structural determination have become necessary.

    Two methods for high throughput analysis of proteins are presented in the first part of this thesis. The first method is the thermofluor method, which presents a fast way to identify stabilizing conditions for a particular protein. It was shown that the addition of a stabilizing additive, identified with the thermofluor method, significantly increased the likelihood of growing protein crystals. The second method presented in this thesis provides a fast and robust way to detect metal containing proteins.

    The second part of this thesis describes the crystal structures of two RNA modifying enzymes, the pseudouridine synthase TruD and the RNA m5C methyltransferase YebU. The catalytic domain of TruD was shown to bear remarkable structural similarity to the other pseudouridine families despite a lack of sequence similarity. In addition to the catalytic domain, the structure of TruD also contained an insertion domain with a novel fold.

    YebU was also found have two structurally distinct domains. The N-terminal catalytic domain has a high structural similarity to other RNA m5C methyltransferases. The C-terminal domain was revealed to be a so-called PUA domain, which had not been predicted by previous sequence alignments.

  • 3.
    Walldén, Karin
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Structural Studies of Human 5'-Nucleotidases2008Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    5’-Nucleotidases (5’NTs) are catabolic enzymes of the nucleotide metabolism. They catalyze dephosphorylation of deoxyribo- and ribonucleoside monophosphates and constitute an important control point in the regulation of intracellular nucleotide pools for the maintenance of correct DNA and RNA synthesis.

    By removing the alfa-phosphate group from a nucleotide, the 5’NTs release the nucleoside to pass the plasma membrane by facilitated diffusion. Depending on the cellular need for nucleotides, the nucleosides can either exit the cell for reuse elsewhere or be imported and subsequently phosphorylated by nucleoside and nucleotide kinases.

    The knowledge of how nucleotides are metabolized has been used for rational design of nucleoside analogues that are used in treatment of cancer and viral diseases. These drugs are phosphorylated within the cell to become active. Their dephosphorylation by 5’NTs might be one of the mechanisms behind the resistance experienced by patients towards such drugs.

    This thesis describes structure-function studies on four of the seven known human 5’-NTs. The focus of the work is on the substrate specificity and regulation of these enzymes. Inactive variants of the mitochondrial and cytosolic deoxynucleotidases and the cytosolic 5’-nucleotidase II were used to characterize the structural basis for their substrate specificity in high detail.

    Based on structures of the apoprotein and activator/activator+substrate complexes of cytosolic 5’-nucleotidase II, a mechanism for the allosteric activation of this enzyme was presented. In this mechanism, the activator induces a conformational change that involves conserved residues of the active site. The conformational change drastically increases the enzyme affinity for the phosphate moiety of the substrate.

1 - 3 of 3
CiteExportLink to result list
Permanent link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf