PDRA - Protein Self-Assembly & Biomineralisation

University of Cambridge; Cambridge; On-site; GBP 38,000 - 45,000; Full time

Job summary

University of Cambridge invites applications for a Postdoctoral Research Associate in the Knowles group, Department of Chemistry, to develop approaches for the control of self-assembly of proteins into 2D and 3D material phases. The project forms part of an ARIA international consortium with cross-department collaboration.

The PDRA will develop protein toolkits for screening proteins enabling controlled nucleation, protection, alignment and locking, and apply the platform to protein–inorganic

Qualifications

• PhD in Physics, Chemistry, Materials Science, biochemistry, or related discipline.
• Experience studying synthesis and/or characterisation of crystalline inorganic materials.
• Sound understanding of microfluidics-based approaches, flow/spray-based patterning, 3D printing and related templating methods.
• Knowledge of protein design, nucleation, self-assembly and biomineralisation.

Responsibilities

• Lead development of techniques to control protein-templated biomineralisation.
• Develop protein toolkits for screening proteins enabling controlled nucleation, protection, alignment and locking.
• Apply platform to synthesis of protein–inorganic magnetic components and nanocrystals using droplet/flow/field processing.
• Supervise PhD and Master’s students and maintain the group’s instruments.

Skills

microfluidics

flow patterning

3D printing

protein design

nucleation

self-assembly

biomineralisation

Education

PhD in a relevant field

Tools

custom instruments

Job description

University of Cambridge invites applications for a Postdoctoral Research Associate in the Knowles group, Department of Chemistry, to develop approaches for the control of self-assembly of proteins into 2D and 3D material phases. The project forms part of an ARIA international consortium with cross-department collaboration.

The PDRA will develop protein toolkits for screening proteins enabling controlled nucleation, protection, alignment and locking, and apply the platform to protein–inorganic