Search Results - (Author, Cooperation:J. R. Winkler)
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1Latest Papers from Table of Contents or Articles in PressStaff View
Publication Date: 2013-03-30Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Animals ; Heme/*chemistry ; Myoglobin/*chemistry ; Spectrophotometry, Ultraviolet/*methods ; Tryptophan/*chemistryPublished by: -
2Latest Papers from Table of Contents or Articles in PressL. Hammarstrom ; J. R. Winkler ; H. B. Gray ; S. Styring
American Association for the Advancement of Science (AAAS)
Published 2011Staff ViewPublication Date: 2011-07-19Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: *Photosynthesis ; *Solar Energy ; Synthetic BiologyPublished by: -
3Articles: DFG German National LicensesSchmid, J. ; Hämmerle, C. H. F. ; Fliickiger, L. ; Winkler, J. R. ; Olah, A. J. ; Gogolewskiz, S. ; Lang, N. P.
Copenhagen : Munksgaard International Publishers
Published 1997Staff ViewISSN: 1600-0501Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: The aim of the present study was to evaluate the effect of natural deproteinized bone mineral on the temporal and spatial pattern of bone formation in a guided bone regeneration model system while using a bioresorbable membrane device. A periosteal skin flap was raised uncovering the calvaria of 20 rabbits. A stiff hemispherical dome made of polylactic acid was placed onto the roughened calvaria and anchored by screws. Prior to placement, the dome was either filled with peripheral blood (control group, 8 rabbits) or with blood and OsteoGraf/N-300 (test group, 12 rabbits). At 1 month, histologic sections revealed bone regeneration in both test and control domes to various degrees. In the test domes, bone height reached 78%(67–83) and bone volume was 11%(&17), while in the control domes, bone height was 45%(1467) and bone volume 6%(1-I 1). At 2 months, bone height was unchanged in the test group at 70%(67–83) and bone volume had only slightly increased to 16%(1 l-2 1). In the controls, height increased to 86%(60–100) and volume to 20%(9–27). Thus, in this model system, natural bone mineral fill contributed to accelerate initial bone neogenesis, while it did not contribute to increasing bone volume or bone height at later observation stages.Type of Medium: Electronic ResourceURL: -
4Articles: DFG German National LicensesWittung-Stafshede, Pernilla ; Hill, Michael G. ; Gomez, Ester ; Di Bilio, A. J. ; Karlsson, B. Göran ; Leckner, Johan ; Winkler, J. R. ; Gray, Harry B. ; Malmström, B. G.
Springer
Published 1998Staff ViewISSN: 1432-1327Keywords: Key words Azurin ; Copper-A ; Cyclic voltammetry ; Protein folding ; Rack-induced coordinationSource: Springer Online Journal Archives 1860-2000Topics: BiologyChemistry and PharmacologyNotes: Abstract Cyclic voltammetry has been used to determine the reduction potentials of blue (Pseudomonas aeruginosa azurin) and purple (Thermus thermophilus CuA domain) copper proteins unfolded by guanidine hydrochloride. These Cu(II/I) potentials [456 (azurin); 453 (CuA) mV vs., NHE] are higher than those of the folded proteins. The downshift of the potential in the folded state can be accounted for by assuming that rack-induced axial coordination stabilizes Cu(II) relative to Cu(I) in a protein-encapsulated active site.Type of Medium: Electronic ResourceURL: -
5Articles: DFG German National LicensesStaff View
ISSN: 1432-1327Source: Springer Online Journal Archives 1860-2000Topics: BiologyChemistry and PharmacologyNotes: Abstract Analysis of electron-transfer (ET) kinetics data obtained from experiments on Ru-modified proteins (cytochrome c, azurin, myoglobin) reveals that distant donor-acceptor electronic couplings depend upon the secondary structure of the intervening polypeptide matrix. Rates of Fe2+→Ru3+ ET reactions in cytochrome c decay exponentially with tunneling-pathway length (decay constant 0.73 Å–1); these rates also decay exponentially with Ru-Fe distance (decay constant 1.1 Å–1). In azurin, a β-sheet protein, Cu+→Ru3+ rates exhibit an exponential Cu-Ru distance dependence with a decay constant of 1.1 Å–1. Comparison of distant couplings in azurin and myoglobin suggests that hydrogen bonds are better mediators across β sheets than through α helices.Type of Medium: Electronic ResourceURL: