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Uppsala, Sweden

We are indebted to Prof. A. Claesson (University of Uppsala, Sweden) for submitting... [Pg.170]

Figure 2.7 (a) Illustration of the twist of (3 sheefs. Befa sfrands are drawn as arrows from the amino end to the carboxy end of the p strand in this schematic drawing of fhe protein thioredoxin from E. coli, fhe sfrucfure of which was defermined in the laboratory of Carl Branden, Uppsala, Sweden, fo 2.8 A resolution. The mixed p sheet is viewed from one of ifs ends, (b) The hydrogen bonds between the P strands in the mixed p sheet of fhe same profein. [(a) Adapfed from B. Furugren.]... [Pg.20]

Figure 4.3 In most a/p-barrel structures the eight p strands of the barrel enclose a tightly packed hydrophobic core formed entirely by side chains from the p strands. The core is arranged in three layers, with each layer containing four side chains from alternate p strands. The schematic diagram shows this packing arrangement in the a/p barrel of the enzyme glycolate oxidase, the structure of which was determined by Carl Branden and colleagues in Uppsala, Sweden. Figure 4.3 In most a/p-barrel structures the eight p strands of the barrel enclose a tightly packed hydrophobic core formed entirely by side chains from the p strands. The core is arranged in three layers, with each layer containing four side chains from alternate p strands. The schematic diagram shows this packing arrangement in the a/p barrel of the enzyme glycolate oxidase, the structure of which was determined by Carl Branden and colleagues in Uppsala, Sweden.
Figure 4.8 The active site in all a/p barrels is in a pocket formed by the loop regions that connect the carboxy ends of the p strands with the adjacent a helices, as shown schematically in (a), where only two such loops are shown, (b) A view from the top of the barrel of the active site of the enzyme RuBisCo (ribulose bisphosphate carboxylase), which is involved in CO2 fixation in plants. A substrate analog (red) binds across the barrel with the two phosphate groups, PI and P2, on opposite sides of the pocket. A number of charged side chains (blue) from different loops as welt as a Mg ion (yellow) form the substrate-binding site and provide catalytic groups. The structure of this 500 kD enzyme was determined to 2.4 A resolution in the laboratory of Carl Branden, in Uppsala, Sweden. (Adapted from an original drawing provided by Bo Furugren.)... Figure 4.8 The active site in all a/p barrels is in a pocket formed by the loop regions that connect the carboxy ends of the p strands with the adjacent a helices, as shown schematically in (a), where only two such loops are shown, (b) A view from the top of the barrel of the active site of the enzyme RuBisCo (ribulose bisphosphate carboxylase), which is involved in CO2 fixation in plants. A substrate analog (red) binds across the barrel with the two phosphate groups, PI and P2, on opposite sides of the pocket. A number of charged side chains (blue) from different loops as welt as a Mg ion (yellow) form the substrate-binding site and provide catalytic groups. The structure of this 500 kD enzyme was determined to 2.4 A resolution in the laboratory of Carl Branden, in Uppsala, Sweden. (Adapted from an original drawing provided by Bo Furugren.)...
Figure S.3 Schematic diagram of the structure of human plasma retinol-binding protein (RBP), which is an up-and-down P barrel. The eight antiparallel P strands twist and curl such that the structure can also be regarded as two p sheets (green and blue) packed against each other. Some of the twisted p strands (red) participate in both P sheets. A retinol molecule, vitamin A (yellow), is bound inside the barrel, between the two P sheets, such that its only hydrophilic part (an OH tail) is at the surface of the molecule. The topological diagram of this stmcture is the same as that in Figure 5.2. (Courtesy of Alwyn Jones, Uppsala, Sweden.)... Figure S.3 Schematic diagram of the structure of human plasma retinol-binding protein (RBP), which is an up-and-down P barrel. The eight antiparallel P strands twist and curl such that the structure can also be regarded as two p sheets (green and blue) packed against each other. Some of the twisted p strands (red) participate in both P sheets. A retinol molecule, vitamin A (yellow), is bound inside the barrel, between the two P sheets, such that its only hydrophilic part (an OH tail) is at the surface of the molecule. The topological diagram of this stmcture is the same as that in Figure 5.2. (Courtesy of Alwyn Jones, Uppsala, Sweden.)...
Salo Gbonowitz, Department of Organic Chemistry, Chemical Institute, University of Uppsala, Uppsala, Sweden... [Pg.481]

Lawrence Livermore National Lab., Livermore, California Condensed Matter Theory Group, Physics Department, Uppsala University, S-75121 Uppsala, Sweden... [Pg.13]

Dr. Igor Abrikosov Condensed Matter Theory Group Institute of Physics University of Uppsala Box 530, S-75121 Uppsala Sweden... [Pg.499]

See brochure of Nobel Committees for Physics and Chemistry, The Royal Swedish Academy of Sciences, List of the Nobel Prize Laureates 1901-1994, Alm-quist Wiksell Tryckeri Uppsala, Sweden, 1995. [Pg.18]

H. Akashi, K. Tanaka, K. Sekai, 5th International Symposium on Polymer Electrolytes, Uppsala, Sweden, August 1996, Poster P-10. [Pg.524]

Roark D, Yphantis DA (1969) Ann New York Acad Sci 164 245 Rinde H (1928) The Distribuhon of the Sizes of Particles in Gold Sols Prepared According to the Nuclear Method. PhD Thesis, University of Uppsala, Uppsala, Sweden Harding SE (1988) Gums and Stabilisers for the Food Industry 4 15 http //www.wyatt.com/... [Pg.252]

Morancho, R., Constant, G., Gallon, C., Boucham, J., Mazerolles, P., and Bernard, C., OMCVD Elaborating and Optical Properties of Germanium Carbon Alloys, Proc. 5th European Conf. on CVD, (J. Carlsson and J. Lindstrom, eds ), pp. 526-532, Univ. of Uppsala, Sweden (1985)... [Pg.230]

Watson, P.F. Plummer, J.M. (1985). The responses of boar sperm membranes to cold shock and cooling. In Deep Freezing of Boar Semen (Johnson, L.A. Larsson, K., eds.), pp. 113-128, Swedish University of Agricultural Sciences, Uppsala, Sweden. [Pg.384]

Institute of Chemistry University of Uppsala 751 21 Uppsala, Sweden (Section 6.7.2.5)... [Pg.27]

A. Guette, M. Barret, R. Naslain, P. Hagenmuller, L. E. Tergenius, T. Lundstrom, 7th. Int. Symp. Boron, Borides, Related Compounds, Uppsala-Sweden, (1981) J. Less-Common Met., 82, 325 (1981). [Pg.243]

Joseph G. Fripiat (95), Laboratoire de Chimie Thdorique Appliquee, Facultds Universitaires Notre-Dame de la Paix, B-5000 Namur, Belgium J. W. Gauld (339), Department of Quantum Chemistry, Uppsala University, S-75120 Uppsala, Sweden... [Pg.384]

The p-lactams (penicillins and their derivatives) are the drugs which most frequently cause IgE-mediated anaphylactic reactions. Diagnosis is based on skin tests. To date, the best vaUdated in vitro diagnostic methods are specific IgE and BAT. As for the determination of specific IgE using ImmimoCap (Phadia AB, Uppsala, Sweden), the sensitivity of the technique in the diagnosis of immediate reaction to (3-lactams with positive skin test ranges, according to the study, from 37 to 54% with a specificity of between 83 and 100% [23,24]. [Pg.129]


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See also in sourсe #XX -- [ Pg.76 , Pg.78 , Pg.85 , Pg.88 , Pg.89 , Pg.92 ]




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