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novel methods of enzymatic nitrogen fixation by repurposing natural metalloenzymes. To achieve this ambitious goal, we will combine computational work (focused on computing electric fields within enzyme
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to function, and this process is tightly regulated by a network of chaperone proteins. At the heart of this network is Hsp90, a molecular chaperone essential for the folding and maturation of at least 20% of
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are causing major changes in the physical environment, which may in turn fundamentally alter the functioning of ecosystems. Alpine and arctic ecosystems have remained relatively natural so far, but
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recruitments (summer and winter) and work closely with the Biozentrum group leaders to maintain and further develop the high-quality standards of our PhD program. You will independently organize and oversee
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to exchange ideas with other doctoral students, receive feedback on the work in progress, and acquire the skills necessary for an academic career. The Doctoral Program also supports its members with
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Your position Biomolecular dynamics, such as conformational changes, are the understudied link between biomolecular structure and function. Single-molecule FRET is an established technique, unique
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100%, starting January 2026 (negotiable) Proteins must fold correctly to function, and this process is tightly regulated by a network of chaperone proteins. At the heart of this network is Hsp90, a
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discipline Strong interest in experimental quantum science and nanotechnology Keen to gain hands-on experience in laboratory research Analytical thinking, motivation, and the ability to work both independently
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function. Single-molecule FRET is an established technique, unique in its capacity to resolve nanometer small conformational changes within single biomolecules (proteins, DNA, RNA), without suffering from
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sciencesYears of Research Experience1 - 4 Additional Information Website for additional job details https://academicpositions.com Work Location(s) Number of offers available1Company/InstituteUniversity