| 1. |
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| 2. |
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| 3. |
- Kannan, K. K., et al.
(author)
-
Bror Erik Strandberg (1930-2018)
- 2018
-
In: Acta Crystallographica Section D. - : International Union Of Crystallography. - 2059-7983. ; 74:7, s. 711-712
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Journal article (pop. science, debate, etc.)
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| 4. |
- Liljas, Anders, et al.
(author)
-
Textbook of structural biology
- 2017. - 2
-
Book (peer-reviewed)abstract
- This book provides a comprehensive coverage of the basic principles of structural biology, as well as an up-to-date summary of some main directions of research in the field. The relationship between structure and function is described in detail for soluble proteins, membrane proteins, membranes, and nucleic acids. There are several books covering protein structure and function, but none that give a complete picture, including nucleic acids, lipids, membranes and carbohydrates, all being of central importance in structural biology. The book covers state-of-the-art research in various areas. It is unique for its breadth of coverage by experts in the fields. The book is richly illustrated with more than 400 color figures to highlight the wide range of structures.
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| 5. |
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| 6. |
- Liljas, Juvas Marianne, et al.
(author)
-
Högskolan Dalarna och folkskoleseminariets historia - Perspektiv på lärarutbildningen i Falun, ca 1875–1970
- 2023
-
In: Svenska Historikermötet i Umeå 14–16 juni 2023. - Umeå.
-
Conference paper (other academic/artistic)abstract
- Svenska Historikermötet i Umeå 14–16 juni 2023Titel: Högskolan Dalarna och folkskoleseminariets historia – Perspektiv på lärarutbildningen i Falun, ca 1875–1970Den som har inflytande över utformandet av en lärarutbildning och blivande lärares kunskapssyn, kan också komma att påverka framtida generationers sätt att se på samhället och världen (Hartman 2012, Bejerot & Hasselbladh 2020). Vid folkskoleseminariet i Falun bedrevs lärarutbildning från etablerandet 1875 fram till det att verksamheten succesivt övergick i lärarhögskolans regi 1968–70. I en mening sammanfaller dessa nära på hundra år av lärarutbildning därmed också med framväxten av det moderna Sverige.I antologiprojektet ’Högskolan Dalarna och folkskoleseminariets historia’ riktas fokus mot en rad tidigare outforskade aspekter av hur seminarietraditionen, i ett specifikt lokalsamhälle, etableras och förändras under olika tidsperioder. Enligt tidigare forskning hade den 1842 inrättade folkskolan uppgiften att legitimera ett traditionellt, religiöst och auktoritärt samhällssystem (Petterson 1993, Lundahl 2005). Längre fram i tiden, inte minst från sekelskiftet 1900 och framåt, kom folkskolan dock att alltmer betraktas som ett centralt redskap i det moderna samhällets utvecklande av medborgares agens, kvinnlig frigörelse och samhällsutveckling (Linne 1996). Under femton år med start 1864 etablerades i Sverige fem folkskoleseminarier för kvinnor. Först ut var Stockholm och Skara som 1864 ombildades från att utbilda män till att utbilda kvinnor. Därefter etablerades folkskollärarinneseminarier i både Falun och Kalmar år 1875 och fyra år senare följde ett femte i Umeå (Sörensen 1942). Seminarieetableringarna i Falun och övriga orter innebar en ökning i andelen kvinnliga lärare under slutet av 1800-talet och i förlängningen kom den patriarkala skolordningen att utmanas (Florin 1987).Beslutet den 30 april 1875 att anlägga ett folkskoleseminarium i Falun, säger något om behovet av lärare på den svenska landsbygden, men också något om Faluns historiska bakgrund som lärdomsstad (Claesson 2015, Liljas 2019:2021, Ödman 1995). Möjligen finns också lokala och aktörsburna förklaringar till den utpräglat progressiva profil som med tiden kom att växa fram vid folkskoleseminariet i Falun (Linné 1996:2006). I projektets delstudier görs exempel på pregnanta avsteg från folkskolans normer av framträdande lärarutbildare som Valborg Olander och Anna Sörensen. Med utgångspunkt i ett mycket rikt arkivmaterial blir det också möjligt att följa hur de och andra lärarutbildare i valet av uppgifter och utformningen av textnära kommentarer söker påverka de blivande lärarinnorna i deras sätt att se på kunskap, undervisning och lärarskap. Utifrån än mer kritiskt orienterade perspektiv på verksamheten granskas också urvalsprinciperna för rekryteringen av nya lärarinnor och interkulturella aspekter av den faktiska verksamheten.Genom dessa nedslag berörs därmed också hur professionaliseringen av läraryrket tar form i relation till ett bildningsanspråk - vilket ofta tycks gravitera mot medborgerliga och könsutjämnande principer. Under den föreslagna sessionen till historikermötet i Umeå presenteras fem av dessa bidrag:Juvas Marianne Liljas presentation fokuserar på Valborg Olanders (1861-1943) reformerande insatser vid folkskoleseminariet i Falun och har titeln ’’’Det varma hjärtat”: Valborg Olanders pedagogiska arv i Faluseminariets historia’.I presentationen ’Folkskolelärarinneseminarier i Sverige: en jämförelse mellan Falun och Umeå, 1875–1915’ intar Emil Marklund en komparativ ansats. Folkskollärarinneseminariet i Umeå grundades 1879, blott fyra år efter seminariet i Falun. Utifrån rubriken ’Kunskaps- och undervisningsideal i förändring: Pedagogiska examensuppsatser vid Falu folkskoleseminarium 1915–1937’ analyserar Anders Persson de skriftliga kommentarer som dåtidens lärarutbildare lämnar på de blivande lärarinnornas texter.I ´En lärare blir till. Om ideal och normer för blivande lärare på folkskollärarseminariet i Falun år 1876–1909´presenterar Ulrika Norburg exempel på hur rekryteringsprocessen av blivande lärarinnor vid seminariet gick till.Anders Blomqvist presentation ’Perspektiv på seminariet i krigs- och brytningstider 1940–1960: genus, klass och etnicitet’ fokuserar på erfarenheter från Faluseminariet under tiden för Andra världskriget och efterföljande år. Ordförande: Simon Lundberg, Umeå universitet.Discussant: Anna Götlind, Stockholms universitet.
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| 7. |
- Petersson, Karin, et al.
(author)
-
Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence
- 2001
-
In: EMBO Journal. - : Wiley. - 0261-4189 .- 1460-2075. ; 20:13, s. 3306-3312
-
Journal article (peer-reviewed)abstract
- The three-dimensional structure of a bacterial superantigen, Staphylococcus aureus enterotoxin H (SEH), bound to human major histocompatibility complex (MHC) class II (HLA-DR1) has been determined by X-ray crystallography to 2.6 Å resolution (1HXY). The superantigen binds on top of HLA-DR1 in a completely different way from earlier co-crystallized superantigens from S. aureus. SEH interacts with high affinity through a zinc ion with the β1 chain of HLA-DR1 and also with the peptide presented by HLA-DR1. The structure suggests that all superantigens interacting with MHC class II in a zinc-dependent manner present the superantigen in a common way. This suggests a new model for ternary complex formation with the T-cell receptor (TCR), in which a contact between the TCR and the MHC class II is unlikely.
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| 8. |
- Al-Karadaghi, Salam, et al.
(author)
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A decade of progress in understanding the structural basis of protein synthesis
- 2000
-
In: Progress in Biophysics and Molecular Biology. - 1873-1732. ; 73:2, s. 167-193
-
Research review (peer-reviewed)abstract
- The key reaction of protein synthesis, peptidyl transfer, is catalysed in all living organisms by the ribosome - an advanced and highly efficient molecular machine. During the last decade extensive X-ray crystallographic and NMR studies of the three-dimensional structure of ribosomal proteins, ribosomal RNA components and their complexes with ribosomal proteins, and of several translation factors in different functional states have taken us to a new level of understanding of the mechanism of function of the protein synthesis machinery. Among the new remarkable features revealed by structural studies, is the mimicry of the tRNA molecule by elongation factor G, ribosomal recycling factor and the eukaryotic release factor 1. Several other translation factors, for which three-dimensional structures are not yet known, are also expected to show some form of tRNA mimicry. The efforts of several crystallographic and biochemical groups have resulted in the determination by X-ray crystallography of the structures of the 30S and 50S subunits at moderate resolution, and of the structure of the 70S subunit both by X-ray crystallography and cryo-electron microscopy (EM). In addition, low resolution cryo-EM models of the ribosome with different translation factors and tRNA have been obtained. The new ribosomal models allowed for the first time a clear identification of the functional centres of the ribosome and of the binding sites for tRNA and ribosomal proteins with known three-dimensional structure. The new structural data have opened a way for the design of new experiments aimed at deeper understanding at an atomic level of the dynamics of the system.
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| 9. |
- Anders, Liljas
(author)
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An enzyme in disguise
- 2020
-
In: IUCrJ. - 2052-2525. ; 7:2, s. 144-145
-
Journal article (peer-reviewed)
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| 10. |
- Ban, Nenad, et al.
(author)
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A new system for naming ribosomal proteins.
- 2014
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In: Current Opinion in Structural Biology. - : Elsevier BV. - 1879-033X .- 0959-440X. ; 24, s. 165-169
-
Journal article (peer-reviewed)abstract
- A system for naming ribosomal proteins is described that the authors intend to use in the future. They urge others to adopt it. The objective is to eliminate the confusion caused by the assignment of identical names to ribosomal proteins from different species that are unrelated in structure and function. In the system proposed here, homologous ribosomal proteins are assigned the same name, regardless of species. It is designed so that new names are similar enough to old names to be easily recognized, but are written in a format that unambiguously identifies them as 'new system' names.
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| 11. |
- Davydova, N, et al.
(author)
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L22 ribosomal protein and effect of its mutation on ribosome resistance to erythromycin
- 2002
-
In: Journal of Molecular Biology. - 1089-8638. ; 322:3, s. 635-644
-
Journal article (peer-reviewed)abstract
- The ribosomal protein L22 is a core protein of the large ribosomal subunit interacting with all domains of the 23 S rRNA. The triplet Met82-Lys83-Arg84 deletion in L22 from Escherichia coli renders cells resistant to erythromycin which is known as an inhibitor of the nascent peptide chain elongation. The crystal structure of the Thermus thermophilus L22 mutant with equivalent triplet Leu82-Lys83-Arg84 deletion has been determined at 1.8 Angstrom resolution. The superpositions of the mutant and the wild-type L22 structures within the 50 S subunits from Haloarcula marismortui and Deinococcus radiodurans show that the mutant beta-hairpin is bent inward the ribosome tunnel modifying the shape of its narrowest part and affecting the interaction between L22 and 23 S rRNA. 23 S rRNA nucleotides of domain V participating in erythromycin binding are located on the opposite sides of the tunnel and are brought to those positions by the interaction of the 23 S rRNA with the L22 P-hairpin. The mutation in the L22 P-hairpin affects the orientation and distances between those nucleotides. This destabilizes the erythromycin-binding "pocket" formed by 23 S rRNA nucleotides exposed at the tunnel surface. It seems that erythromycin, while still being able to interact with one side of the tunnel but not reaching the other, is therefore unable to block the polypeptide growth in the drug-resistant ribosome. (C) 2002 Elsevier Science Ltd. All rights reserved.
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| 12. |
- Fedorov, R V, et al.
(author)
-
Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins
- 2001
-
In: Acta Crystallographica. Section D: Biological Crystallography. - 1399-0047. ; D57:7, s. 968-976
-
Journal article (peer-reviewed)abstract
- The crystal structure of Thermus thermophilus ribosomal protein TL5 in complex with a fragment of Escherichia coli 5S rRNA has been determined at 2.3 Å resolution. The protein consists of two domains. The structure of the N-terminal domain is close to the structure of E. coli ribosomal protein L25, but the C-terminal domain represents a new fold composed of seven -strands connected by long loops. TL5 binds to the RNA through its N-terminal domain, whereas the C-terminal domain is not included in this interaction. Cd2+ ions, the presence of which improved the crystal quality significantly, bind only to the protein component of the complex and stabilize the protein molecule itself and the interactions between the two molecules in the asymmetric unit of the crystal. The TL5 sequence reveals homology to the so-called general stress protein CTC. The hydrophobic cores which stabilize both TL5 domains are highly conserved in CTC proteins. Thus, all CTC proteins may fold with a topology close to that of TL5.
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| 13. |
-
From a grain of salt to the ribosome : the history of crystallography as seen through the lens of the Nobel Prize
- 2015
-
Editorial collection (other academic/artistic)abstract
- This book is published to celebrate the International Year of Crystallography 2014, as proclaimed by the United Nations. The year has been chosen as the International Year of Crystallography since it was 100 years ago that the first Nobel Prize was awarded for crystallographic observations to Max von Laue. Just a year later, Sir William Henry Bragg and William Lawrence Bragg, father and son, won their prize for showing the possibility of determining atomic positions in crystals. This book describes the lives and works of 33 Nobel Laureates starting with Wilhelm Conrad Röntgen (1901) and ending with Brian Kobilka (2012). It also reproduces the most important works of these scientists. The book gives a historical perspective of a scientific field that is important for our understanding of the atomic organization of the world around us, from inorganic materials to complex biological molecules, such as the ribosome.
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| 14. |
- Gao, Rong, et al.
(author)
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Deep sequencing reveals global patterns of mRNA recruitment during translation initiation
- 2016
-
In: Scientific Reports. - : Springer Science and Business Media LLC. - 2045-2322. ; 6
-
Journal article (peer-reviewed)abstract
- In this work, we developed a method to systematically study the sequence preference of mRNAs during translation initiation. Traditionally, the dynamic process of translation initiation has been studied at the single molecule level with limited sequencing possibility. Using deep sequencing techniques, we identified the sequence preference at different stages of the initiation complexes. Our results provide a comprehensive and dynamic view of the initiation elements in the translation initiation region (TIR), including the S1 binding sequence, the Shine-Dalgarno (SD)/anti-SD interaction and the second codon, at the equilibrium of different initiation complexes. Moreover, our experiments reveal the conformational changes and regional dynamics throughout the dynamic process of mRNA recruitment.
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| 15. |
- Grela, Przemysłw, et al.
(author)
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Structural characterization of the ribosomal P1A-P2B protein dimer by small-angle X-ray scattering and NMR spectroscopy
- 2007
-
In: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 46:7, s. 1988-1998
-
Journal article (peer-reviewed)abstract
- The five ribosomal P-proteins, denoted P0-(P1-P2)(2), constitute the stalk structure of the large subunit of eukaryotic ribosomes. In the yeast Saccharomyces cerevisiae, the group of P1 and P2 proteins is differentiated into subgroups that form two separate P1A-P2B and P1B-P2A heterodimers on the stalk. So far, structural studies on the P-proteins have not yielded any satisfactory information using either X-ray crystallography or NMR spectroscopy, and the structures of the ribosomal stalk and its individual constituents remain obscure. Here we outline a first, coarse-grained view of the P1A-P2B solution structure obtained by a combination of small-angle X-ray scattering and heteronuclear NMR spectroscopy. The complex has an elongated shape with a length of 10 nm and a cross section of similar to 2.5 nm. N-15 NMR relaxation measurements establish that roughly 30% of the residues are present in highly flexible segments, which belong primarily to the linker region and the C-terminal part of the polypeptide chain. Secondary structure predictions and NMR chemical shift analysis, together with previous results from CD spectroscopy, indicate that the structured regions involve alpha-helices. NMR relaxation data further suggest that several helices are arranged in a nearly parallel or antiparallel topology. These results provide the first structural comparison between eukaryotic P1 and P2 proteins and the prokaryotic L12 counterpart, revealing considerable differences in their overall shapes, despite similar functional roles and similar oligomeric arrangements. These results present for the first time a view of the structure of the eukaryotic stalk constituents, which is the only domain of the eukaryotic ribosome that has escaped successful structural characterization.
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| 16. |
- Hansson, Sebastian, et al.
(author)
-
Crystal structure of a mutant elongation factor G trapped with a GTP analogue
- 2005
-
In: FEBS Letters. - : Wiley. - 1873-3468 .- 0014-5793. ; 579:20, s. 4492-4497
-
Journal article (peer-reviewed)abstract
- Elongation factor G (EF-G) is a G protein factor that catalyzes the translocation step in protein synthesis on the ribosome. Its GTP conformation in the absence of the ribosome is currently unknown. We present the structure of a mutant EF-G (T84A) in complex with the non-hydrolysable GTP analogue GDPNP. The crystal structure provides a first insight into conformational changes induced in EF-G by GTP. Comparison of this structure with that of EF-G in complex with GDP suggests that the GTP and GDP conformations in solution are very similar and that the major contribution to the active GTPase conformation, which is quite different, therefore comes from its interaction with the ribosome. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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| 17. |
- Hansson, Sebastian, et al.
(author)
-
Structural insights into fusidic acid resistance and sensitivity in EF-G
- 2005
-
In: Journal of Molecular Biology. - : Elsevier BV. - 1089-8638 .- 0022-2836. ; 348:4, s. 939-949
-
Journal article (peer-reviewed)abstract
- Fusidic acid (FA) is a steroid antibiotic commonly used against Gram positive bacterial infections. It inhibits protein synthesis by stalling elongation factor G (EF-G) on the ribosome after translocation. A significant number of the mutations conferring strong FA resistance have been mapped at the interfaces between domains G, III and V of EF-G. However, direct information on how such mutations affect the structure has hitherto not been available. Here we present the crystal structures of two mutants of Thermus thermophilus EF-G, G16V and T84A, which exhibit FA hypersensitivity and resistance in vitro, respectively. These mutants also have higher and lower affinity for GTP respectively than wild-type EF-G. The mutations cause significant conformational changes in the switch 11 loop that have opposite effects on the position of a key residue, Phe90, which undergoes large conformational changes. This correlates with the importance of Phe90 in FA sensitivity reported in previous studies. These structures substantiate the importance of the domain G/domain III/domain V interfaces as a key component of the FA binding site. The mutations also cause subtle changes in the environment of the "P-loop lysine", Lys25. This led us to examine the conformation of the equivalent residue in all structures of translational GTPases, which revealed that EF-G and eEF2 form a group separate from the others and suggested that the role of Lys25 may be different in the two groups. (c) 2005 Elsevier Ltd. All rights reserved.
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| 18. |
- Helgstrand, Magnus, et al.
(author)
-
The ribosomal stalk binds to translation factors IF2, EF-Tu, EF-G and RF3 via a conserved region of the L12 C-terminal domain
- 2007
-
In: Journal of Molecular Biology. - : Elsevier BV. - 0022-2836 .- 1089-8638. ; 365:2, s. 468-479
-
Journal article (peer-reviewed)abstract
- Efficient protein synthesis in bacteria requires initiation factor 2 (IF2), elongation factors Tu (EF-Tu) and G (EF-G), and release factor 3 (RF3), each of which catalyzes a major step of translation in a GTP-dependent fashion. Previous reports have suggested that recruitment of factors to the ribosome and subsequent GTP hydrolysis involve the dimeric protein L12, which forms a flexible "stalk" on the ribosome. Using heteronuclear NMR spectroscopy we demonstrate that L12 binds directly to the factors IF2, EF-Tu, EF-G, and RF3 from Escherichia coli, and map the region of L12 involved in these interactions. Factor-dependent chemical shift changes show that all four factors bind to the same region of the C-terminal domain of L12. This region includes three strictly conserved residues, K70, L80, and E82, and a set of highly conserved residues, including V66, A67, V68 and G79. Upon factor binding, all NMR signals from the C-terminal domain become broadened beyond detection, while those from the N-terminal domain are virtually unaffected, implying that the C-terminal domain binds to the factor, while the N-terminal domain dimer retains its rotational freedom mediated by the flexible hinge between the two domains. Factor-dependent variations in linewidths further reveal that L12 binds to each factor with a dissociation constant in the millimolar range in solution. These results indicate that the L12-factor complexes will be highly populated on the ribosome, because of the high local concentration of ribosome-bound factor with respect to L12.
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| 19. |
- Hirokawa, G, et al.
(author)
-
Post-termination complex disassembly by ribosome recycling factor, a functional tRNA mimic
- 2002
-
In: EMBO Journal. - : Wiley. - 1460-2075. ; 21:9, s. 2272-2281
-
Journal article (peer-reviewed)abstract
- Ribosome recycling factor (RRF) together with elongation factor G (EF-G) disassembles the post- termination ribosomal complex. Inhibitors of translocation, thiostrepton, viomycin and aminoglycosides, inhibited the release of tRNA and mRNA from the post-termination complex. In contrast, fusidic acid and a GTP analog that fix EF-G to the ribosome, allowing one round of tRNA translocation, inhibited mRNA but not tRNA release from the complex. The release of tRNA is a prerequisite for mRNA release but partially takes place with EF-G alone. The data are consistent with the notion that RRF binds to the A-site and is translocated to the P-site, releasing deacylated tRNA from the P- and E-sites. The final step, the release of mRNA, is accompanied by the release of RRF and EF-G from the ribosome. With the model post-termination complex, 70S ribosomes were released from the post-termination complex by the RRF reaction and were then dissociated into subunits by IF3.
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| 20. |
- Hunter Lindqvist, Steven, 1959-
(author)
-
What and How Students Perceive They Learn When Doing Mini-Companies in Upper Secondary School
- 2017
-
Licentiate thesis (other academic/artistic)abstract
- The aim of this study is to gain more in-depth knowledge into what Swedish upper secondary school students perceive they learn, and the factors that students perceive affect learning, when they start and run mini-companies within the Junior Achievement Company Program. The data is comprised of interviews with eleven students each of whom ran a mini-company with other students. Situated learning theory, experiential learning theory and theoretical concepts on reflection in learning were used to analyze and further understand the data.The results reveal that the students talk about, and appear to convey, equal importance upon learning general skills as learning business skills when doing their mini-companies. Students describe using general skills they improved while running their mini-companies in other school activities and non-school activities leading to better performance in these activities. Doing business activities triggers learning and provides students with an opportunity to further develop, and learn multiple aspects, of skills.Students identify many factors, such as time, autonomy, assessment, and deadlines, which they associate with their mini-companies. On the whole, they say these factors have a positive effect on learning both business and general skills, however some factors can also inhibit learning. An analysis of all the factors students identified reveals that they originate, or are influenced by, multiple contexts such as school, the Swedish Junior Achievement organization, and the business environment. Together these factors can be said to create a special school community of practice for their mini-company project. Students point out significant differences between their mini-company project, and other school projects they have previously done, thus providing valuable insight into the importance of project design in relation to learning skills and possible pedagogical implications regarding learning general skills in other school projects.
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| 21. |
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| 22. |
- Jonsson, Bengt-Harald, et al.
(author)
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Perspectives on the Classical Enzyme Carbonic Anhydrase and the Search for Inhibitors
- 2020
-
In: Biophysical Journal. - : Elsevier BV. - 0006-3495 .- 1542-0086. ; 119:7, s. 1275-1280
-
Research review (peer-reviewed)abstract
- Carbonic anhydrase (CA) is a thoroughly studied enzyme. Its primary role is the rapid interconversion of carbon dioxide and bicarbonate in the cells, where carbon dioxide is produced, and in the lungs, where it is released from the blood. At the same time, it regulates pH homeostasis. The inhibitory function of sulfonamides on CA was discovered some 80 years ago. There are numerous physiological-therapeutic conditions in which inhibitors of carbonic anhydrase have a positive effect, such as glaucoma, or act as diuretics. With the realization that several isoenzymes of carbonic anhydrase are associated with the development of several types of cancer, such as brain and breast cancer, the development of inhibitor drugs specific to those enzyme forms has exploded. We would like to highlight the breadth of research on the enzyme as well as draw the attention to some problems in recent published work on inhibitor discovery.
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| 23. |
- Kjellsson, Anders
(author)
-
Om bildningens utmaningar och möjligheter i den svenska grundskolan
- 2022
-
Licentiate thesis (other academic/artistic)abstract
- The aim of this study is to develop new knowledge about the challenges and possibilities of Bildung in the Swedish compulsory school. Based on a qualitative analysis of five elite interviews with five theorists of Bildung, this study is inspired by curriculum theory and, in particular, the key analytical concepts of curriculum models, frame factors and room for freedom The results make visible both challenges and possibilities for Bildung in the Swedish compulsory school. First, through a thematic analysis, five themes were identified: i) Bildung as an open process; ii) Bildung in relation to coherence and overview; iii) Bildung and meaning making; iv) Bildung in education; and v) Bildung as resistance. This thematic analysis has shown that tensions exist between Bildung and the measurable results that are the focus in the Swedish school. Furthermore, a one-sided alignment to measurability tends to neglect several dimensions of Bildung. Second, the outcomes from the thematic analysis were considered in light of the curriculum theory framework in the form of an additional analysis based on three theoretical curriculum models. Using the theoretical concepts frame factors and room for freedom, the analysis demonstrates that various curriculum models, in different ways, both restrict Bildung and make it possible. Despite this, the results illustrate how Bildung, to a greater or lesser extent, can be operationalized through different curriculum models. The third analysis reveals a shift in the understanding of Bildung in the Swedish school, from something differential to something for every pupil. The final results are visualized as three “windows” of Bildung, each of which presents how Bildung can be a natural component of the Swedish compulsory school: i) a democratized and expanded view of Bildung; ii) a fluid dialogue between the subjective and objective dimensions of Bildung; and iii) Bildung as resistance. This study contributes to a current and forward-looking discussion about the role of Bildung, with a special focus on the Swedish compulsory school; however, it is also of relevance outside the Swedish context.
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| 24. |
- Kristensen, O, et al.
(author)
-
Is tRNA binding or tRNA mimicry mandatory for translation factors?
- 2002
-
In: Current Protein and Peptide Science. - 1875-5550. ; 3:1, s. 133-141
-
Research review (peer-reviewed)abstract
- tRNA is the adaptor in the translation process. The ribosome has three sites for tRNA, the: A-, P-, and E-sites. The tRNAs bridge between the ribosomal subunits with the decoding site and the mRNA on the small or 30S subunit and the peptidyl transfer site on the large or 50S subunit. The possibility that, translation release factors could mimic tRNA has been discussed for a long time, since their function is very similar to that of tRNA. They identify stop codons of the mRNA presented in the decoding site and hydrolyse the nascent peptide from the peptidyl tRNA in the peptidyl transfer site. The structures of eubacterial release factors are not yet known, and the first example of tRNA mimicry was discovered when elongation factor G (EF-G) was found to have a closely similar shape to a complex of elongation factor Tu (EF-Tu) with aminoacyl-tRNA. An even closer imitation of the tRNA shape is seen in ribosome recycling factor (RRF). The number of proteins mimicking tRNA is rapidly increasing. This primarily concerns translation factors. It is now evident that in some sense they are either tRNA mimics, GTPases or possibly both.
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| 25. |
- Kristensen, O, et al.
(author)
-
Structural characterization of the stringent response related exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family
- 2004
-
In: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 43:28, s. 8894-8900
-
Journal article (peer-reviewed)abstract
- Exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GPPA) enzymes play central roles in the bacterial stringent response induced by starvation. The high-resolution crystal structure of the putative Aquifex aeolicus PPX/GPPA phosphatase from the actin-like ATPase domain superfamily has been determined, providing the first insights to features of the common catalytic core of the PPX/GPPA family. The protein has a two-domain structure with an active site located in the interdomain cleft. Two crystal forms were investigated (type I and 11) at resolutions of 1.53 and 2.15 Angstrom, respectively. This revealed a structural flexibility that has previously been described as a "butterfly-like" cleft opening around the active site in other actin-like superfamily proteins. A calcium ion is observed at the center of this region in type I crystals, substantiating that PPX/GPPA enzymes use metal ions for catalysis. Structural analysis suggests that nucleotides bind at a similar position to that seen in other members of the superfamily.
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