Tentativt kvantitativ analys av högskoleverkets utvärderingar av utbildningskvalitet år 2011-2012.

En kvantitativ analys av Högskoleverkets (HSV) utvärderingar av utbildningskvalitet har genomförts såväl beskrivande som med försök till statistisk prövning av tänkbara samband mellan olika kvantitativa variabler och nyckeltal karaktäriserande universiteten och högskolornas verksamhet. Ett sammanvägt mått "Utbildningskvalitet" för de olika lärosätena bildades baserat på de av HSV för respektive utbildning använda omdömena "Bristande kvalitet" (= 1 p), "Hög kvalitet" (= 2 p) och "Mycket hög kvalitet" (= 3 p). "Utbildningskvaliteten" kan därmed arbiträrt anta ett värde mellan 1 till 3 där ett högre värde anger en högre bedömd kvalitet. De i juli 2012 av HSV publicerade utvärderingarna av 481 olika utbildningar/examina vid 28 st lärosäten ingick i den deskriptiva redovisningen. För statistiska test av eventuella samband mellan "Utbildningskvalitet" och olika kvantitativa variabler och nyckeltal eller skillnader mellan olika grupperingar av lärosätena inkluderades enbart de 17 st lärosäten som hade tio eller fler utvärderingar genomförda (totalt 429 utvärderingar). Resultaten av de statistiska analyserna indikerar att den i HSV:s utvärderingar gjorda bedömningen av utbildningarnas kvalitet ("Utbildningskvalitet") positivt samvarierar med hur mycket forskning ett lärosäte har uttryckt i absoluta ekonomiska tal. Det finns ett negativt men statistiskt säkerställt samband mellan bedömd "Utbildningskvalitet" och hur mycket utbildning ett lärosäte har i relativa tal i förhållande till forskning. Ju högre andel forskning, ju högre bedömd "Utbildningskvalitet". Något statistiskt säkerställt samband mellan den av HSV bedömda kvaliteten i utbildningen och antalet studenter, total ekonomisk omsättning eller graden av lärosätenas uppdragsutbildning återfanns inte. När lärosätena grupperades i de två kategorierna "Universitet" respektive "Högskolor" återfanns ingen statistiskt säkerställd skillnad i bedömd "Utbildningskvalitet" mellan kategorierna. Vid en gruppering av lärosätena i de två kategorierna "Äldre universitet" (inrättade före 1999) respektive "Nya universitet och högskolor" erhölls en statistiskt säkerställd skillnad med högre bedömd "Utbildningskvalitet" för gruppen "Äldre universitet". Då studien enbart omfattar de första 19 av de av HSV planerade drygt hundra bedömda huvudområdena så kan studien rimligen inte anses som representativ och generaliserbar för hela högskolesektorns olika utbildningsområden. Denna studie måste därför betraktas som tentativ och av mer hypotesgenererande karaktär.QC 20130130</p

1H^1H and 13C^{13}C NMR investigations of N,N'-bis(2- and 3-pyridinyl)-2,6-pyridine dicarboxamides

$^IH NMR$ spectra of N,N'-bis(2-pyridinyl)-2,6- pyridinedicarboxamides (1 to 3) and N,N'-bis(3-pyridinyl)-2,6-pyridinedicar- boxamide (4) have been analysed using the COSY spectra. Accurate IH chemical shifts and coupling constants have been obtained from the simulation of the resolution enhanced spectra. $^{13}C NMR$ spectra were analysed with the help of HETCORR and proton coupled $^{13}C$ spectra. The $^{13}C-^H$ coupling constants were obtained by the simulation of the proton coupled $^{13}C NMR$ spectra. From $^1H NMR$ spectra and NOE enhancements, it is inferred that the two 2-pyridyl rings of 1 to 3 are coplanar with the amide plane, while the 3-pyridyl ring of 4 is out of the amide plane

Proton and carbon-13 NMR studies of conformational preferences in N-(2-pyridinyl)-2-pyridinecarboxamides

The H-1 and C-13 NMR spectra, molecular conformation and intermolecular association of N-(2-pyridinyl)-2-pyridinecarboxamides and 2-pyridinecarboxamide are discussed. The H-1 NMR spectra have been analyzed with the aid of COSY spectra and the C-13 spectra with the aid of HETCOR, proton coupled spectra and C-13-H-1 coupling constants. In concentrated CDCl3 solution, N-(2-pyridinyl)-2-pyridinecarboxamides dimerise by intermolecular association

1H and 13C NMR spectra of some unsymmetric N,N-dipyridyl ureas: spectral assignments and molecular conformation

Abstract: The H-1 NMR spectra of N-(2-pyridyl), N'-(3-pyridyl)ureas and N-(2-pyridyl), N'-(4-pyridyl)ureas in CDCl3 and (CD3)(2)CO have been assigned with the aid of COSY and NOE experiments and chemical shift and coupling constant correlations, The C-13 NMR spectra in CDCl3 were analysed utilizing the HETCOR and proton coupled spectra, The H-1 NMR spectra, NOE effects and MINDO/3 calculations have been utilized to show that the molecular conformation of these compounds has the 2-pyridyl ring coplanar with the urea plane with the N-H group hydrogen bonded to the nitrogen of the 2-pyridyl group on the other urea nitrogen while the 3/4-pyridyl group rotates rapidly about the N-C-3/N-C-4 bond

Localized agglutinin staining in muscle capillaries from normal and very old atrophic human muscle using winged bean (Psophocarpus tetragonolobus) lectin

The winged bean (Psophocarpus tetragonolobus) agglutinin (total lectin) and its basic (WBA I) and acidic isoform (WBA II) were used to analyze capillaries in sections from human muscle. The microvessels were clearly labeled after incubation with the lectins in both normal muscle and in old muscles with age-related type II atrophy or muscle fiber grouping. Muscle fibers, nerves, and connective tissue remained unstained. The total lectin detected muscle capillaries from all blood group AB0 individuals. The isoform WBA I reacted only with blood vessels in blood group A and B individuals, while the blood vessels in blood group 0 individuals were demonstrated with WBA II. WBA I staining was inhibited by p-nitrophenyl α-galactopyranoside and N-acetylgalactosamine, whereas 2'-fucosyllactose and preincubation with an antibody against type-1 chain H abolished capillary staining with WBA II. The study demonstrates the usefulness of WBA as a marker of capillaries in human muscle

On the relationship of thermodynamic parameters with the buried surface area in protein-ligand complex formation

Prediction of thermodynamic parameters of protein-protein and antigen-antibody complex formation from high resolution structural parameters has recently received much attention, since an understanding of the contributions of different fundamental processes like hydrophobic interactions, hydrogen bonding, salt bridge formation, solvent reorganization etc. to the overall thermodynamic parameters and their relations with the structural parameters would lead to rational drug design. Using the results of the dissolution of hydrocarbons and other model compounds the changes in heat capacity (DeltaCp), enthalpy (DeltaH) and entropy (DeltaS) have been empirically correlated with the polar and apolar surface areas buried during the process of protein folding/unfolding and protein-ligand complex formation. In this regard, the polar and apolar surfaces removed from the solvent in a protein-ligand complex have been calculated from the experimentally observed values of changes in heat capacity (DeltaCp) and enthalpy (DeltaH) for protein-ligand complexes for which accurate thermodynamic and high resolution structural data are available, and the results have been compared with the x-ray crystallographic observations. Analyses of the available results show poor correlation between the thermodynamic and structural parameters. Probable reasons for this discrepancy are mostly related with the reorganization of water accompanying the reaction which is indeed proven by the analyses of the energetics of the binding of the wheat germ agglutinin to oligosaccharides

NMR study of the conformation of N-(3-pyridinyl)-2- pyridinecarboxamide, N-(3-pyridinyl)acetamide and 2-pyridinecarboxamide

The $^IH$ NMR spectra of N-(3-pyridinyl)-2-pyridinecarboxamide (1), N-(3-pyridinyl)acetamide (2) and 2-pyridinecarbox- amide (3) in $CDCI_3$, $(CD_3)_2CO$ and $CD_3CN$ have been measured and analyzed by utilising the correlations in the COSY and HETCOR spectra, chemical shifts and coupling constants. $^1H$ NMR spectra in dilute solutions $(\sim1 mg \hspace {2mm}ml^{-1})$ and NOE experiments suggest (1) to occur in a single conformation with the 2-pyridyl ring coplanar with the amide plane and the 2-pyridyl nitrogen hydrogen bonded intramolecularly to the N-H. In concentrated solutions of $CDCl_3$ and $(CD_3)_2CO$, (1) dimerises by cooperative hydrogen bonding. The structure of the dimer was inferred to be similar to that of the adenine- adenine (A-A) base-pair

On the relationship of thermodynamic parameters with the buried surface area in protein-ligand complex formation

Prediction of thermodynamic parameters of protein-protein and antigen-antibody complex formation from high resolution structural parameters has recently received much attention, since an understanding of the contributions of different fundamental processes like hydrophobic interactions, hydrogen bonding, salt bridge formation, solvent reorganization etc. to the overall thermodynamic parameters and their relations with the structural parameters would lead to rational drug design. Using the results of the dissolution of hydrocarbons and other model compounds the changes in heat capacity (ΔC<SUB>p</SUB>), enthalpy (ΔH) and entropy (ΔS) have been empirically correlated with the polar and apolar surface areas buried during the process of protein folding/unfolding and protein-ligand complex formation. In this regard, the polar and apolar surfaces removed from the solvent in a protein-ligand complex have been calculated from the experimentally observed values of changes in heat capacity (ΔC<SUB>p</SUB>) and enthalpy (ΔH) for protein-ligand complexes for which accurate thermodynamic and high resolution structural data are available, and the results have been compared with the X-ray crystallographic observations. Analyses of the available results show poor correlation between the thermodynamic and structural parameters. Probable reasons for this discrepancy are mostly related with the reorganization of water accompanying the reaction which is indeed proven by the analyses of the energetics of the binding of the wheat germ agglutinin to oligosaccharides

Localized agglutinin staining in muscle capillaries from normal and very old atrophic human muscle using winged bean ( Psophocarpus tetragonolobus ) lectin

The winged bean (Psophocarpus tetragonolobus) agglutinin (total lectin) and its basic (WBA I) and acidic isoform (WBA II) were used to analyze capillaries in sections from human muscle. The microvessels were clearly labeled after incubation with the lectins in both normal muscle and in old muscles with age-related type II atrophy or muscle fiber grouping. Muscle fibers, nerves, and connective tissue remained unstained. The total lectin detected muscle capillaries from all blood group AB0 individuals. The isoform WBA I reacted only with blood vessels in blood group A and B individuals, while the blood vessels in blood group 0 individuals were demonstrated with WBA II. WBA I staining was inhibited by p-nitrophenyl α-galactopyranoside and N-acetylgalactosamine, whereas 2′-fucosyllactose and preincubation with an antibody against type-1 chain H abolished capillary staining with WBA II. The study demonstrates the usefulness of WBA as a marker of capillaries in human muscle