This symposium is held within the frame of the collaborative network SFB 677 based at the Christiana Albertina University of Kiel (CAU). It has been organized to support and encourage women to aim at and pursue a career in science by exploring and unfolding their own strengths and qualities. Expert women from different countries and from complementary fields have been invited to highlight diverse aspects of gender equality and discuss individual career development opportunities. The aim of the meeting is to empower men and women to discover and overcome unconscious perceptions and stereotypes in science (and beyond) as well as to provide practical hints and a chance for networking.
08:30
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Uta Wille
Melbourne, Australia
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Research Involving Environmental Free Radical Oxidants – A Journey from Germany to Australia
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The chemistry of atmospheric free radicals has been the ‘red threat’ of my research since my graduation at the University of Kiel many years ago, and which brought me to the University of Melbourne 12 years ago. Like many other countries, Australia ‘suffers’ from serious underrepresentation of women in the STEM disciplines. Whereas in Australia about 50% of the Bachelor of Science graduates are women, their numbers are steadily declining after the Postdoc level, and only very few women are pursuing an academic career. This presentation will outline briefly my career pathway to this date. Possible strategies to improve gender balance in scientific careers will be outlined, which have been the focus during my role as Assistant Dean for Staff Equal Opportunity of the Faculty of Science of the University of Melbourne.
Uta Wille graduated from her PhD in Science at the University of Kiel, Germany, in 1993. Her PhD thesis was performed in the area of Atmospheric Chemistry. She changed her research directions when she was offered a position for a Habilitation in Organic Chemistry at the same institution, which was completed in 1999. In 1997/98 she undertook a Postdoctoral Fellowship with Professor Bernd Giese at the University of Basel, Switzerland. In 1999, she was appointed as Privatdozent at the University of Kiel and was invited in 2000 as a Visiting Fellow in the School of Chemistry at The University of Melbourne. In January 2003, Uta Wille moved permanently to Australia, where she was appointed as a Lecturer in the School of Chemistry at The University of Melbourne. In 2006, she was promoted to Senior Lecturer and in 2011 to Associate Professor and Reader at the same institution. Uta Wille is a Chief Investigator in the ARC Centre of Excellence for Free Radical Chemistry and Biotechnology. Her research program targets the chemistry of reactive intermediates by merging radicals of atmospheric importance with organic and bio-organic chemistry.
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09:15
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Marie Körner
Paris, France
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Three very good reasons for becoming a scientist
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“Female scientists have made steady gains in recent decades but they face persistent career challenges.” This is how begins Helen Shen her paper in Nature on inequalities between men and women in science.[1] In spite of this disturbing observation, during my talk, I will report my personal experience as a scientist and hope to share my enthusiasm for science and for research in particular. I will also discuss the situation of French versus German women in this field, and plead for a better communication of the scientific community with other citizens.
[1] Inequality quantified: Mind the gender gap. Helen Shen 2013, Nature 495, 7439, News feature.
Marie Körner was educated and trained in Paris. She is a molecular biologist and Research Director at the CNRS (National Center for Scientific Research). During her research career she studied several biological systems in France and in the United States. In 1989, returning from the NCI/NIH, she created a research team at the CNRS in Paris, that studied the NF-κB/Rel family of transcription factors, that she headed for 17 years. Since 2006 she got involved in the management and scientific communication of research Centers.
Marie was trained as a biochemist and molecular biologist and got her PhD in Paris from the «Pierre & Marie Curie» University (UPMC), while studying the structure-function relationship of myosin from heart and skeletal muscles (1983). After obtaining her PhD, she joined a neuropharmacology laboratory in INSERM headed by Jean-Charles Schwartz. This first postdoctoral training gave her the opportunity to study histamine H1 receptors in the brain. She synthesized iodobolpyramine, the first iodinated antagonist of histamine, and a powerful tool for the characterization and mapping of H1 receptors in the brain (1983-85). After that, she joined the Immunology Department at the Pasteur Institute in Paris, where she used her expertise in protein biochemistry to characterize soluble factors involved in B cell activation (1985-87). During this initial experience in “molecular immunology” she realized that the space between the cell membrane and the nucleus was basically a black box. Her interest in the study of signal transduction involved in cell activation and differentiation, motivated her to join William Farrar’s lab as “visiting scientist” at the NCI (Frederick, Maryland, USA) in 1987, to study the transduction of activating signals in T lymphocytes. She was particularly interested in molecules that were bridging cytoplasmic events to the initiation of transcription in the nuclear compartment, using the HIV promoter region as probe. Her research at NCI evidenced that the newly discovered transcription factor NF-κB in B cells, was a key mediator of activating signals in T lymphocytes, and she provided initial molecular characterization of this ubiquitous transcription factor. Back in Paris, Marie became member of CNRS, established her research team working on functions and regulations of the NF κB/Rel family of transcription factors in normal and pathological conditions. Her major contributions are discoveries of alternative pathways leading to the activation of atypical NF-κB members, identification of new pathological forms of NF-κB, elucidation of several functions of NF-κB in T cells in vivo. Today, Marie is a CNRS senior scientist which mission is to organize and stimulate scientific communication of scientific research centers.
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10:00
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coffee break
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10:30
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Beate Koksch
Berlin, Germany
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The coiled coil architecture – peptide switches and the multivalent presentation of carbohydrates
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Since joining Freie Universität Berlin in 2004, the Koksch group has established a research program aimed at understanding and influencing peptide and protein structure and function. For example, the Koksch group has developed a set of highly versatile peptide models that enables the systematic evaluation of how mutations in the primary structure influence the stability of the quarternary structures formed by -helices and -strands. The design of these peptides took advantage of one of the most widespread and best known folding motifs occurring in nature: The α-helical coiled coil. Coiled coils typically consist of right-handed amphiphilic α-helices that are wound around each other forming a left-handed superhelix. The primary structure is characterized by a periodicity of seven residues, the so-called 4-3 heptad repeat (abcdefg)n. Positions a and d are typically occupied by apolar residues that form a hydrophobic core at the interface of the helices. Positions e and g are frequently occupied by charged amino acids that form interhelical electrostatic interactions. The remaining heptad repeat positions b, c and f, are exposed to the solvent and their free functional groups can therefore be modified by hydrophobic residues to induce an ambiguity in the structure formation or can be used for the conjugation of ligands. The structural simplicity and regularity of the coiled-coil motif allow for the predictable positioning and, thus, presentation of ligands.
Conformational transitions are a crucial factor in the vast majority of protein misfolding diseases. In most of these cases, the change in conformation is accompanied by the formation of insoluble aggregates, which often precludes a detailed characterization at the molecular level. Transitions are extraordinarily complex processes that are to date not fully understood on a molecular level. Therefore, much effort has been put into the development of simplified, easy-to-synthesize peptide models that can be used to elucidate the molecular processes that underlie the conformational switch.
This talk introduces coiled coil-based, switchable peptides developed by our laboratory. These peptides are accessible using the repertoire of bioorganic and peptide chemists and are organized according to different external stimuli that initiate and control the structural transition. These model systems have been shown to serve well in following the conversion of secondary structures depending on factors such as pH, ionic strength, metal ions, chaperones or solvents. The strategies introduced here additionally exhibit outstanding potential for the development of novel, self-assembling bio-inspired materials.
The self-assembling properties of the coiled coil folding motif also form the foundation for the second topic of this talk which concerns its application for the multivalent presentation of peptide and carbohydrate ligands. Part one of this topic focuses on the multivalent presentation of a peptide epitope and an antigenic glycan on a coiled coil-based, self-assembling peptide scaffold. We showed that the coiled coil scaffold retains the ability to self-assemble into α-helical fibers when loaded with both ligands, and that both peptide and carbohydrate ligands are optimally accessible for binding with appropriate partners. A host of immunological and imaging techniques were used to determine binding of antibodies and lectins to these ligands in the presence or absence of this multivalent scaffold. Enhanced antibody binding for both, the peptide epitope and the carbohydrate antigen were detected when conjugated to the fiber-forming peptide. The results of this study suggest that this peptide scaffold can find application in the context of bio-assays or in vitro diagnostics.
In the second part of this study, the utility of the coiled-coil motif as rational tool for the presentations of ligands is discussed. To target the unknown structure of the asialoglycoprotein receptor (ASGP-R), a library of fifteen glycopeptides carrying up to three galactose moieties, either directly on the backbone or via spacers with two different length was generated. The recognition of the glycopeptide library by the ASGP-R was tested in whole-cell assays by fluorescence assisted cell sorting (FACS).
Professor Beate Koksch studied Chemistry and Biochemistry at the University Leipzig and was Postdoc with Professor Reza M Ghadiri and Professor Carlos F Barbas, III. Since 2004, she has been Professor for Organic and Natural Product Chemistry at the Freie Universität Berlin. Her group studies complex folding mechanisms that occur in neurodegenerative diseases, develops new multivalent scaffolds and investigates fluorinated amino acids.
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11:15
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Eva Sophia Myers
Odense, Denmark
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Privilege Walk Activity – with 15 volunteers from the auditory. Discussion.
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11:45
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Eva Sophia Myers Martin Svensson
Odense, Denmark
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Handling stereotypes, differences and diversity in Academia – experiences and reflections from the daily life at the Faculty of Science, University of Southern Denmark
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In relation to and extension of our participation in FESTA Female Empowerment in Science and Technology Academia, we will present how we as a Science Faculty work towards a more balanced gender representation among our scientific staff and in the faculty management. This takes place through initiatives to foster inclusive, diverse and collaborative working environments, decision making processes, mentoring practices and meeting cultures as well as through more formal measures such as committees, administrative procedures, action plans, and monitoring activities.
Our approach hinges on a basic understanding that we need all hands, hearts and heads; that diverse groups working on creative problem solving produce better and richer outcomes; and that the STEM-disciplines worldwide at present and in the near foreseeable future are bleeding qualified people. We believe that this is largely due to tight and historically conditioned norms for who fits in and is entitled – which in turn excludes many others in both overt and covert, intentional and unconscious ways. This easily leads to a dynamic where those who differ from the norm are seriously undervalued, are not recognized as fitting in, and – most critically – do not themselves have a sense of entitlement and are continually and subliminally confirmed in an unhealthy alienation. This is all the more critical as it occurs in patterns that are not immediately visible to individuals – individuals who have an impact on others and who make large and small life decisions based on stereotypes and biased perceptions. One large such group is women, and our standpoint is that problems, which women in Academia encounter, point to structural issues, which – if they are solved – will benefit everyone: staff, students, academia and society as a whole.
Our presentation will include a short experiential, the privilege walk, where together we can explore the interplay between norms, stereotypes and diversity.
I am head of the faculty administration at the Faculty of Science, University of Southern Denmark. With a background in goldsmithing, linguistics, psychology and organizational consulting, my approach to university administration and governance focuses on communication, collaboration, organizational and leadership development. My main professional interest is how an organization can appreciate differences and diversity and how it is possible in a university setting to establish and nurture a culture that allows for the interplay and creative output of these differences. To my mind a gender focus is one – but not the only – important aspect of ensuring diversity in research, science and the academic setting. I am the local project leader of FESTA Female Empowerment in Science and Technology Academia, a five-year implementation project under EU’s FP7-program concerned with attracting, promoting and keeping more women at all levels of the academic career in the Science disciplines.
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12:15
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panel discussion
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13:15
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Tanja M. Wrodnigg
Graz, Austria
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Challenges of Diversity
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Tanja M. Wrodnigg graduated from Technical University in Graz, Austria, and received her PhD in Science in 1999 from the same University. In 2006 she finished her Habiliation in Organic Chemistry with a thesis entitled “Fresh Synthetic Approaches in Glycoscience: Synthesis towards Biological Active Carbohydrates and Analogues and Their Evaluation as Tools for Bioscience”. She held several positions at TU Graz before she became University Assistant at the Institute of Organic Chemistry. Next she was appointed Assistant Professor and since 1999 she is Associate Professor for Organic Chemistry at the Institute for Organic Chemistry at Technical University Graz. She was a Visiting Scientist at Alchemia Pty Ltd in Brisbane, Australia, and Visiting Professor at the University of British Columbia in Vancouver and at Technical University of Denmark in Kopenhagen. Her research is centered around specialized carbohydrate chemistry, investigation of Amadori rearrangement and the development of glycosidase inhibitors. In addition to her activities in research and university teaching, she is Vice-chairperson of the University’s Working Committee for Gender Equality (AkG).
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14:00
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lunch reception and networking
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15:00
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end of symposium
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