Protein-Templated Materials Scientist (Postdoc)

RFCSR

Sheffield

Hybrid

GBP 38,000 - 46,000

Full time

3 days ago
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Benefits offered by this job

Annual leave (41 days)
Pension scheme
Flexible working
Parenting / Caring leave

Job summary

The University of Sheffield seeks a Postdoctoral Research Associate with expertise in proteins as materials to advance protein-templated synthesis and metal oxide sintering.

Work focuses on protein-mediated, low-temperature sintering methods for oxide materials, using protein-mediated assembly to control monolith growth and protein microstructure, accompanied by comprehensive characterization to assess chemical, physical, and functional properties.

Qualifications

  • Honours degree in a relevant subject area.
  • PhD in Materials Science, Chemical Engineering, Biological Engineering, Biomaterials, or a closely related field.
  • Right to work in the UK or eligibility under UK Visa & Immigration guidelines.

Responsibilities

  • Conduct protein-mediated assembly research to control monolith growth in functional oxide materials.
  • Characterize samples and maintain detailed lab logs.
  • Collaborate with the PI, co-investigators, and project partners.
  • Plan, schedule, and execute experiments to meet project milestones.
  • Prepare reports and present findings at meetings and conferences.
  • Stay current with literature and publish manuscripts.
  • Adhere to Health & Safety policies and CoSHH protocols.
  • Embed sustainability and ethical practices in daily work.

Skills

Communication
Independent work
Teamwork
Planning

Education

Honours degree in relevant subject
PhD in Materials Science or related field

Tools

Microsoft Office

Job description

The University of Sheffield seeks a Postdoctoral Research Associate with expertise in proteins as materials to advance protein-templated synthesis and metal oxide sintering.

Work focuses on protein-mediated, low-temperature sintering methods for oxide materials, using protein-mediated assembly to control monolith growth and protein microstructure, accompanied by comprehensive characterization to assess chemical, physical, and functional properties.

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