30 results match your criteria: "1 Universitetsvej[Affiliation]"
Biochim Biophys Acta
May 2006
Department of Life Science and Chemistry, Roskilde University, MEMPHYS-Center for Biomembrane Physics, 1 Universitetsvej, DK-4000 Roskilde, Denmark.
We have performed molecular dynamics simulations to investigate the structure and dynamics of charged bilayers as well as the distribution of counterions at the bilayer interface. For this, we have considered the negatively charged di-myristoyl-phosphatidyl-glycerol (DMPG) and di-myristoyl-phosphatidyl-serine (DMPS) bilayers as well as a protonated di-myristoyl-phosphatidyl-serine (DMPSH) bilayer. We were particularly interested in calcium ions due to their important role in biological systems.
View Article and Find Full Text PDFLangmuir
May 2005
Department of Life Sciences and Chemistry, Roskilde University, 1 Universitetsvej, P.O. Box 260, DK-4000 Roskilde, Denmark.
The interaction of cutinase from Humicula insolens (HiC) and sodium dodecyl sulfate (SDS) has been investigated by small-angle neutron scattering (SANS) and isothermal titration calorimetry (ITC). The concerted interpretation of structural and thermodynamic information for identical systems proved valuable in attempts to elucidate the complex modes of protein-detergent interaction. Particularly so at the experimental temperature 22 degrees C, where the formation of SDS micelles is athermal (deltaH = 0), and the effects of protein-detergent interactions stand out clearly in the thermograms.
View Article and Find Full Text PDFBiochim Biophys Acta
August 2004
Department of Life Sciences and Chemistry, Roskilde University, 1 Universitetsvej, Building 18.1, PO Box 260, DK-4000, Denmark.
The interaction free energy of dimethyl sulfoxide (DMSO) and two types phospholipid membranes has been assessed from measurements of vapor pressure. The lipids were phosphatidyl cholines with respectively (14:0/14:0) (DMPC) and (16:0/18:1) (POPC) fatty acid chains. The results were expressed in terms of the iso-osmolal preferential interaction parameter, Gamma(mu1), which remained negative under all experimental conditions investigated here.
View Article and Find Full Text PDFBiochim Biophys Acta
November 2003
Department of Life Sciences and Chemistry, Roskilde University, P.O. Box 260, 1-Universitetsvej, DK-4000 Roskilde, Denmark.
The thermal stability of a recombinant alpha-amylase from Bacillus halmapalus alpha-amylase (BHA) has been investigated using circular dichroism spectroscopy (CD) and differential scanning calorimetry (DSC). This alpha-amylase is homologous to other Bacillus alpha-amylases where crystallographic studies have identified the existence of three calcium binding sites in the structure. Denaturation of BHA is irreversible with a T(m) of approximately 89 degrees C and DSC thermograms can be described using a one-step irreversible model.
View Article and Find Full Text PDFMult Scler
April 2001
Department of Life Sciences and Chemistry, Roskilde University, 1 Universitetsvej, DK-4000 Roskilde, Denmark.
Multiple sclerosis (MS) has been associated with the human leukocyte antigen DR15 allele in Caucasians of North and Central European origin. However, the relative effect of the DR15 homozygous and the DR15 heterozygous genotypes on the disease susceptibility is unclear. Based upon results from three North European studies we have examined this by meta-analysis.
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