71 structures "https:" "https:" "https:" "https:" "https:" "Helmholtz Zentrum Hereon" research jobs in Finland
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period ends: 2026-05-20 23:59 Where to apply Website https://academicpositions.com/ad/tampere-university/2026/postdoctoral-researche… Requirements Research FieldHistoryYears of Research Experience4 - 10
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microeconomics. The position is fixed term for three years with a six-month trial period. The position is part of a new research project “Generational Change for Productive Structural Transformation in Agriculture
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research plan, awards) Further information Home page of the research group: http://www.utu.fi/cyber For further information about the position, please contact: Associate Professor Kaitai Liang, kaitai.liang
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Randomness and Structures; and Geometric analysis, stochastics and partial differential equations, interactions and applications. The starting date is flexible, preferably no later than September 2026
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Turku (http://www.turku.fi/en ) offers language showers and pre-schooling in English. Subsidized private daycare centres also offer daycare in French, English or Russian. Moreover, the Turku International
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of Management Studies at Aalto University School of Business (http://management.aalto.fi ). The department comprises several highly competitive research groups in organization and management theory, strategy
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requirements for pursuing a doctoral degree at the University of Helsinki can be found at https://www.helsinki.fi/en/research/doctoral-education/eligibility-and-educational-documents . The chosen applicant is
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? Please make sure that your ORCID-profile (https://orcid.org ) works: your publications are listed and public (Set visibility: Everyone). You cannot apply to this job without an ORCID profile
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and Finland. How to apply? Please make sure that your ORCID-profile (https://orcid.org ) works: your publications are listed and public (Set visibility: Everyone). You cannot apply to this job without
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-based products. The work will involve the quantification of available niacin and the potential bound forms of niacin by employing a combination of hydrolyses and structure identification using LC-MS