Do UK universities communicate their brands effectively through their websites?

This paper attempts to explore the effectiveness of UK universities’ websites. The area of branding in higher education has received increasing academic investigation, but little work has researched how universities demonstrate their brand promises through their websites. The quest to differentiate through branding can be challenging in the university context, however. It is argued that those institutions that have a strong distinctive image will be in a better position to face a changing future. Employing a multistage methodology, the web pages of twenty UK universities were investigated by using a combination of content and multivariable analysis. Results indicated ‘traditional values’ such as teaching and research were often well communicated in terms of online brand but ‘emotional values’ like social responsibility and the universities’ environments were less consistently communicated, despite their increased topicality. It is therefore suggested that emotional values may offer a basis for possible future online differentiation

The peptide N alpha-(L-alanyl-D-isoglutaminyl)-N epsilon-(D-isoasparaginyl)-L-lysyl-D-alanine and the disaccharide N-acetylglucosaminyl-beta-1,4-N-acetylmuramic acid in cell wall peptidoglycan of Streptococcus faecalis strain ATCC 9790

A major portion of the cell wall peptidoglycan in Streptococcus faecalis is composed of the disaccharide tetrapeptide β-1,4-N-acetylglucosaminyl-N-acetylmuramyl-Nα-(L-alanyl-D-isoglutaminyl)-L-lysyl-D-alanine. The tetrapeptides are cross-linked through single D-isoasparaginyl residues extending from the C-terminal D-alanine of one tetrapeptide unit to the Nє-terminal L-lysine of another. It is the first time that the occurrence of an isoasparaginyl residue in a natural product has been described. The Streptomyces SA en-dopeptidase cleaves D-alanyl-D-isoasparaginyl linkages and is thus the first enzyme known to hydrolyze D-D peptide bonds. Treatment of the disaccharide Nα-( L-alanyl-D-isoglutaminyl)-N є-(D-isoasparaginyl)- L-lysil-D-alanine with 10 equiv of NaOH at 37° for 1 hr results in deamidation of the isoasparaginyl residue together with migration of the aspartyl-lysine peptide bond giving rise to a mixture of Nє-(β-aspartyl)- and N є-(α-aspartyl)lysyl peptides. Under the same alkaline treatment, the N-acetylmuramyl residue undergoes a lactyl elimination which results in the production of acyl peptides and a Morgan-Elson prochromogenic compound, without hydrolysis of the glycosidic linkage. This conversion, interpreted to be the result of a β elimination, also occurs in the other disaccharide peptide monomers previously isolated from Staphylococcus aureus, Micrococcus roseus, and Streptococcus pyogenes

Abbrandgeschwindigkeit von Vollholz, Brettschichtholz und Holzwerkstoffen Schlussbericht fuer die Zeit vom 01.06.89 bis 31.07.92

Available from TIB Hannover: RN5905(2484) / FIZ - Fachinformationszzentrum Karlsruhe / TIB - Technische InformationsbibliothekSIGLEDEGerman