英國利茲大學(xué)2023年招聘博士后職位（聚糖生物物理學(xué)）

利茲大學(xué)（University of Leeds），是一所位于英國利茲的公立綜合性研究型大學(xué)、世界百強(qiáng)名校，英國紅磚大學(xué)，是羅素大學(xué)集團(tuán)，世界大學(xué)聯(lián)盟、國際大學(xué)氣候聯(lián)盟、歐洲大學(xué)協(xié)會(huì)、英聯(lián)邦大學(xué)協(xié)會(huì)、中英大學(xué)工程教育與研究聯(lián)盟、RENKEI、N8大學(xué)聯(lián)盟、白玫瑰大學(xué)聯(lián)盟成員。利茲大學(xué)商學(xué)院獲AACSB、EQUIS和AMBA三重認(rèn)證，是全球商學(xué)院網(wǎng)絡(luò)、“一帶一路”商學(xué)院聯(lián)盟、中歐商校聯(lián)盟成員。

Research Fellow in Glycan Biophysics

University of Leeds

Job Description

Are you an ambitious researcher looking for your next challenge? Do you have an established background in biomolecular analysis by atomic force microscopy and/or optical microscopy, and an interest to decipher complex interactions of polysaccharides and proteins? Do you want to further your career in one of the UK’s leading research intensive universities?

Revealing complexity of hyaluronan-protein interactions

The large, linear and regular polysaccharide hyaluronan (HA) is present in the extracellular matrix of all mammalian tissues, and exhibits an astonishingly broad array of functions in physiology and pathology. The ways in which the HA biopolymer is differentially organised through its interaction with proteins on the cell surface and in the extracellular matrix is key to the diversity of its biological functions. However, the underpinning molecular mechanisms are not well understood, due to the lack of tools to probe the complexity of HA/protein interactions. This project will generate a new toolkit required to reveal the biophysical phenomena underpinning HA/protein interactions and will open up new avenues for regenerative medicine.

The Research Fellow will deploy designer HA molecules with site-specific tags for anchorage and visualisation to develop biophysical assays capable of probing (i) how protein binding relies on HA chain orientation, topology and length, (ii) unconventional interaction modes such as one-dimensional sliding along the HA chain, and (iii) the mechanical response of supramolecular HA/protein complexes. The assays will improve our molecular understanding of HA-protein interactions relevant to immune and inflammatory responses, and tissue development, homeostasis and repair. The combination of method development and applications will provide exceptional career development opportunities for the interested applicant in the growing glycoscience and glycobiophysics areas.

You must have a PhD or be close to completion in biological physics, biophysical chemistry, bioengineering or a related discipline. You should be a highly motivated individual with extensive experience in the analysis of biomolecules and their interactions by advanced atomic force microscopy and/or optical microscopy techniques, and in working across disciplines such as biology, physics and chemistry.

The University of Leeds and the Faculty of Biological Sciences are committed to providing equal opportunities for all and offer a range of family friendly policies. The University is a charter member of Athena SWAN (the national body that promotes gender equality in higher education), and the Faculty of Biological Sciences was awarded a Silver award in 2020. We are proud to be an inclusive Faculty that values all staff, and are happy to consider job share applications and requests for flexible working arrangements from our employees. Our Athena SWAN webpage provides more information.

To explore the post further or for any queries you may have, please contact:

Dr. Ralf Richter, Project Principal Investigator and Associate Professor

Email: r.richter@leeds.ac.uk

Location: Leeds - Main Campus

Faculty/Service: Faculty of Biological Sciences

School/Institute: School of Biomedical Sciences

Category: Research

Grade: Grade 7

Salary: £37,099 to £44,263 per annum

Due to funding limitations, it is unlikely an appointment will be made above £40,521

Working Time: 100%

Post Type: Full Time

Contract Type: Fixed Term (2 years and 10 months due to external funding)

Release Date: Tuesday 08 August 2023

Closing Date: Tuesday 05 September 2023

Reference: FBSBM1195

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