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Associate (PostDoc) to join the Compiler Lab in the Department of Computer Science and Technology at the University of Cambridge, UK. You will work with a team of students and collaborators on the development
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. This research aims to develop a novel method for conjugating oligonucleotides to antibodies, utilizing divinylpyridine motifs. The project will develop skills in both organic synthesis and chemical biology. We
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the proteins associated with their binding sites with a view to understanding therapeutic mechanisms [e.g. see Nature Biotechnology 2023, 41 1265]. We are expanding this work to create methods to characterise
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situ, with direct structure determination, and (ii) investigating and optimizing methods for chirality determination using electron crystallography. Candidate We are looking for a highly motivated and
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. Current Mass Spectrometry approaches have been unable to assess most of the FOXA1 protein for PMTs, but new Mass Spectrometry methods such as 'top-down' approaches permit an unprecedented opportunity
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The Centre for Doctoral Training in Nanoscience and Nanotechnology (NanoDTC) at the University of Cambridge invites applications for its 3.5-year interdisciplinary PhD programme. The programme
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Department/Location: Department of Biochemistry, Central Cambridge PhD Position - Marie Curie network ON-Tract: Protein engineering of enzymes: in vitro directed evolution and machine learning-based elaboration of biocatalysis for synthesis. A doctoral position is available for 3-years to work...
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particularly wide skills training, including experimental and computational work. Applicants should thus have a first (or upper second) class degree in chemistry, biochemistry or a related, relevant subject
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both sites. The project sits at the interface of cell line engineering, protein science and machine learning and you will receive advanced training in these areas while developing methods to accelerate
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Ascl1 are important. We have undertaken a comprehensive discovery experiment to identify all the proteins that can physically interact with Ascl1, using a method we developed called RIME (Rapid