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  • 1.
    Gunnarsson, Svante
    et al.
    Linköpings universitet, Institutionen för systemteknik, Reglerteknik. Linköpings universitet, Tekniska fakulteten.
    Swartz, Maria
    Linköpings universitet, Universitetsförvaltningen.
    On the connectons between the CDIO framework and challenge-based learning2022Ingår i: Proceedings of the 50th SEFI Annual Conference, 2022Konferensbidrag (Refereegranskat)
    Abstract [en]

    Challenge-based learning (CBL) is a learning approach that has received increased attention during  the last years. In some of the publications about CBL the connections to the CDIO (conceive-design-implement-operate) framework is discussed, and the purpose of this paper is to discuss these connections further. CBL has connections to both Problem-based learning (PBL) and Project-based learning (PjBL), but while these are learning approaches, the CDIO framework has a program perspective, including aspects of learning approaches, and hence a wider scope. The connections and differences between CBL and CDIO are discussed based on the components of the CDIO Standards.  

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  • 2.
    Gunnarsson, Svante
    et al.
    Linköpings universitet, Institutionen för systemteknik, Reglerteknik. Linköpings universitet, Tekniska fakulteten.
    Swartz, Maria
    Linköpings universitet, Universitetsförvaltningen.
    Applying the CDIO framework when developing the ECIU University2021Ingår i: Proceedings of the 17th International CDIO Conference / [ed] Jens Bennedsen, Kristina Edström, María Sigríður Guðjónsdóttir Ingunn Sæmundsdóttir ,Natha Kuptasthien, Janne Roslöf, Angkee Sripakagorn, 2021, s. 106-115Konferensbidrag (Refereegranskat)
    Abstract [en]

    The use of the CDIO framework in the development of the ECIU University is presented. The paper discusses the relatively moderate adaptations and modifications of the CDIO Syllabus and Standards that are necessary to make the documents applicable also in this context. Since challenge-based learning (CBL) is central learning format in the ECIU University, special attention is given to the connections between CBL method, the conceive-design-implement-operate sequence and project-based learning, which is central in the CDIO framework. The paper presents both general aspects and examples of the applications and activities within ECIU University and Linköping University (LiU). The main messages of the paper are that the development of the ECIU University will benefit from applying the CDIO framework since it offers references for what an education should give, in terms of knowledge and skills, and how an education program should be designed. In addition, the components of the CDIO framework require a moderate amount of adaptation to be directly applicable. Examples of the ongoing implementation activities at LiU. 

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  • 3.
    Österlund, Marie
    et al.
    Linköpings universitet, Institutionen för fysik, kemi och biologi. Linköpings universitet, Tekniska högskolan.
    Persson, E
    Carlsson, Uno
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi.
    Freskegård, P-O
    Svensson, Magdalena
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi.
    Sequential coagulation factor VIIa domain binding to tissue factor2005Ingår i: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 337, nr 4, s. 1276-1282Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Vessel wall tissue factor (TF) is exposed to blood upon vascular damage which enables association with factor VIIa (FVIIa). This leads to initiation of the blood coagulation cascade through localization and allosteric induction of FVIIa procoagulant activity. To examine the docking pathway of the FVIIa-TF complex, various residues in the extracellular part of TF (sTF) that are known to interact with FVIIa were replaced with cysteines labelled with a fluorescent probe. By using stopped-flow fluorescence kinetic measurements in combination with surface plasmon resonance analysis, we studied the association of the resulting sTF variants with FVIIa. We found the docking trajectory to be a sequence of events in which the protease domain of FVIIa initiates contact with sTF. Thereafter, the two proteins are tethered via the first epidermal growth factor-like and finally the γ-carboxyglutamic acid (Gla) domain. The two labelled sTF residues interacting with the protease domain of FVIIa bind or become eventually ordered at different rates, revealing kinetic details pertinent to the allosteric activation of FVIIa by sTF. Moreover, when the Gla domain of FVIIa is removed the difference in the rate of association for the remaining domains is much more pronounced. © 2005 Elsevier Inc. All rights reserved.

  • 4.
    Österlund, Marie
    et al.
    Linköpings universitet, Institutionen för fysik, kemi och biologi. Linköpings universitet, Tekniska högskolan.
    Persson, E
    Svensson, Magdalena
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi.
    Carlsson, Uno
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi.
    Freskegård, P-O
    Transition state analysis of the complex between coagulation factor VIIa and tissue factor: Suggesting a sequential domain-binding pathway2005Ingår i: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 327, nr 3, s. 789-793Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Injury of a blood vessel exposes membrane-bound tissue factor (TF) to blood, which allows binding of coagulation factor VIIa (FVIIa). This initiation of the coagulation cascade is dictated by a specific multi-domain interaction between FVIIa and TF. To examine the energies involved in the transition state of the FVIIa:TF complex, various residues in the extracellular part of TF (sTF) that are known to interact with FVIIa were replaced with a smaller cysteine residue. Determination of Φ values in each of the positions using surface plasmon resonance measurements enabled us to characterize the transition state complex between the resulting sTF variants and FVIIa. We found that the interactions in the transition state seemed to be most pronounced between the protease domain of FVIIa and sTF while detailed specific interactions between the Gla-domain and sTF were missing. Thus, the transition state energy data indicate a sequential binding event between these two macromolecules. © 2004 Elsevier Inc. All rights reserved.

  • 5.
    Carlsson, Karin
    et al.
    Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi. Linköpings universitet, Tekniska högskolan.
    Osterlund, Maria
    University Holding, Teknikringen 7, SE-581 83 Linköping, Sweden.
    Persson, Egon
    Vascular Biochemistry, Novo Nordisk A/S, Novo Nordisk Park, DK-2760 Måløv, Denmark.
    Freskgard, P.-O.
    Freskgård, P.-O., Protein Biotechnology, Novo Nordisk A/S, Novo Allé, DK-2880 Bagsværd, Denmark, Molecular Biology, Maxygen ApS, DK-2970, Hørsholm, Denmark.
    Carlsson, Uno
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi.
    Svensson, Magdalena
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi.
    Site-directed fluorescence probing to dissect the calcium-dependent association between soluble tissue factor and factor VIIa domains2003Ingår i: Biochimica et Biophysica Acta - Proteins and Proteomics, ISSN 1570-9639, E-ISSN 1878-1454, Vol. 1648, nr 1-2, s. 12-16Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    We have used the site-directed labeling approach to study the Ca 2+-dependent docking of factor VIIa (FVIIa) to soluble tissue factor (sTF). Nine Ca2+ binding sites are located in FVIIa and even though their contribution to the overall binding between TF and FVIIa has been thoroughly studied, their importance for local protein-protein interactions within the complex has not been determined. Specifically we have monitored the association of the ?-carboxyglutamic acid (Gla), the first EGF-like (EGF1), and the protease domains (PD) of FVIIa to sTF. Our results revealed that complex formation between sTF and FVIIa during Ca2+ titration is initiated upon Ca2+ binding to EGF1, the domain containing the site of highest Ca2+ affinity. Besides we showed that a Ca 2+-loaded Gla domain is required for an optimal association of all domains of FVIIa to sTF. Ca2+ binding to the PD seems to be of some importance for the docking of this domain to sTF. © 2003 Elsevier Science B.V. All rights reserved.

  • 6.
    Osterlund, Maria
    et al.
    Novo Nordisk AS, Prot Biotechnol, DK-2880 Bagsvaerd, Denmark Linkoping Univ, IFM, Dept Chem, Linkoping, Sweden Linkoping Univ, IFM, Dept Phys Chem, Linkoping, Sweden Novo Nordisk AS, Vasc Biochem, Malov, Denmark.
    Owenius, Rikard
    Linköpings universitet, Institutionen för fysik, kemi och biologi. Linköpings universitet, Tekniska högskolan.
    Carlsson, Karin
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi.
    Carlsson, Uno
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi.
    Persson, Egon
    Vascular Biochemistry, Novo Nordisk A/S, Denmark.
    Lindgren, Mikael
    Department of Laser Systems, Division of Sensor Technology, Swedish Defence Research Agency, P.O. Box 1165, SE- 581 11 Linko¨ping, Sweden..
    Freskgård, Per-Ola
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi.
    Svensson, Magdalena
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi.
    Probing inhibitor-induced conformational changes along the interface between tissue factor and factor VIIa2001Ingår i: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 40, nr 31, s. 9324-9328Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Upon injury of a blood vessel, activated factor VII (FVIIa) forms a high-affinity complex with its allosteric regulator, tissue factor (TF), and initiates blood clotting. Active site-inhibited factor VIIa (FVIIai) binds to TF with even higher affinity. We compared the interactions of FVIIai and FVIIa with soluble TF (sTF). Six residues in sTF were individually selected for mutagenesis and site-directed labeling. The residues are distributed along the extensive binding interface, and were chosen because they are known to interact with the different domains of FVIIa. Fluorescent and spin probes were attached to engineered Cys residues to monitor local changes in hydrophobicity, accessibility, and rigidity in the sTF-FVIIa complex upon occupation of the active site of FVIIa. The results show that inhibition of FVIIa caused the structures around the positions in sTF that interact with the protease domain of FVIIa to become more rigid and less accessible to solvent. Thus, the presence of an active site inhibitor renders the interface in this region less flexible and more compact, whereas the interface between sTF and the light chain of FVIIa is unaffected by active site occupancy.

  • 7.
    Owenius, Rikard
    et al.
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi.
    Osterlund, Marie
    Linköpings universitet, Institutionen för fysik, kemi och biologi. Linköpings universitet, Tekniska högskolan.
    Svensson, Magdalena
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi.
    Lindgren, M
    Persson, E
    Freskgård, Per-Ola
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi.
    Carlsson, Uno
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi.
    Spin and fluorescent probing of the binding interface between tissue factor and factor VIIa at multiple sites2001Ingår i: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 81, nr 4, s. 2357-2369Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The specific complex between the extracellular part of tissue factor (sTF) and factor Vlla (FVlla) was chosen as a model for studies of the binding interface between two interacting proteins. Six surface-exposed positions in sTF, residues known to contribute to the sTF-FVlla interaction, were selected for cysteine mutation and site-directed labeling with spin and fluorescent probes. The binding interface was characterized by spectral data from electron paramagnetic resonance (EPR) and steady-state and time-domain fluorescence spectroscopy. The labels reported on compact local environments at positions 158 and 207 in the interface region between sTF and the gamma -carboxyglutamic acid (Gla) domain of FVlla, and at positions 22 and 140 in the interface region between sTF and the first epidermal growth factor-like (EGF1) domain of FVlla. The tightness of the local interactions in these parts of the interface is similar to that seen in the interior of globular proteins. This was further emphasized by the reduced local polarity detected by the fluorescent label upon FVlla binding, especially in the sTF-Gla region. There were indications of structural rigidity also at positions 45 and 94 in the interface region between sTF and the protease domain (PD) of FVlla, despite the perturbed cofactor function of these sTF variants. The results of the present study indicate that the multi-probing approach enables comparison of the tightness and characteristics of interaction along the binding interface of a protein complex. This approach also increases the probability of acquiring reliable structural data that are descriptive of the wild-type proteins.

  • 8.
    Osterlund, Marie
    et al.
    Linköpings universitet, Institutionen för fysik, kemi och biologi. Linköpings universitet, Tekniska högskolan.
    Owenius, Rikard
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi.
    Svensson, Magdalena
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi.
    Lindgren, M
    Persson, E
    Freskgård, Per-Ola
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi.
    Carlsson, Uno
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi.
    Mapping local interactions and resolving association kinetics for a receptor-ligand system2000Konferensbidrag (Övrigt vetenskapligt)
  • 9.
    Osterlund, Marie
    et al.
    Linköpings universitet, Institutionen för fysik, kemi och biologi. Linköpings universitet, Tekniska högskolan.
    Owenius, Rikard
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi.
    Persson, E.
    Tissue Factor/Factor VII Research, Novo Nordisk A/S, Måløv, Denmark.
    Lindgren, M.
    Linköpings universitet, Institutionen för fysik, kemi och biologi. Linköpings universitet, Tekniska högskolan.
    Carlsson, Uno
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi.
    Freskgard, P.-O.
    Freskgård, P.-O., Tissue Factor/Factor VII Research, Novo Nordisk A/S, Måløv, Denmark.
    Svensson, Magdalena
    Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi.
    Spectroscopic probing of the influence of calcium and the Gla domain on the interaction between the first EGF domain in factor VIla and tissue factor2000Ingår i: European Journal of Biochemistry, ISSN 0014-2956, E-ISSN 1432-1033, Vol. 267, nr 20, s. 6204-6211Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The binding of factor VIIa (FVIIa) to tissue factor (TF) initiates blood coagulation. The binary complex is dependent on Ca2+ binding to several sites in FVIIa and is maintained by multiple contacts distributed throughout the various domains. Although the contributions from various residues and domains, including the Ca2+ coordination, to the global binding energy have been characterized, their importance for specific local interactions is virtually unknown. To address this aspect, we have attached four spectroscopic probes to an engineered Cys residue replacing Phe140 in soluble TF (sTF). This allows the monitoring of local changes in hydrophobicity and rigidity upon complex formation at the interface between the first epidermal growth factor-like (EGF1) domain of FVIIa and sTF. The fluorescent labels used sense a more hydrophobic environment and the spin labels are dramatically immobilized when FVIIa binds sTF. The results obtained with a 4-carboxy-glutamic acid (Gla)-domainless derivative of FVIIa indicate that the Gla domain has no or minimal influence on the interaction between EGF1 and sTF. However, there is a difference in local Ca2+ dependence between Gla-domainless and full-length FVIIa.

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