[NMR] solid-state NMR postdoc position available

Dear NMR community;

A postdoctoral position is available in my laboratory at UC Irvine (please see attached description.) The project involves developing and using multidimensional sequences for incorporating 2H into protein structure determination experiments in solids, using our unique quadruple-resonance MAS probe operating at 800 MHz. Anyone who is interested should email Rachel Martin (rwmartin@uci.edu). The formal application can be found on UCI’s website at https://recruit.ap.uci.edu/JPF05254. I will also be at the Alpine conference in Chamonix if any potential candidates who are attending the meeting would like to discuss the project with me.


Rachel Martin


School of Physical Sciences

Department of Chemistry

Position: Postdoctoral Position – Solid-State NMR

A postdoctoral position is available at the University of California, Irvine in the area of protein structure determination by solid-state NMR, specifically of the aggregates of eye lens proteins found in cataract disease. The goal of this NIH-funded project is to develop and use advanced solid-state NMR methods for the study of complicated protein aggregates. The group has access to an 800 MHz instrument, equipped with solution-state and MAS probes, including a unique crossed-coil 1H/13C/2H/15N MAS probe purpose-built for these experiments. We also have two dedicated 500 MHz NMR instruments (one solids and one liquids), as well as a fully-equipped molecular biology

laboratory for sample preparation. The ideal candidate will be experienced in protein structure determination by MAS and interested in using novel instrumentation to solve biological problems.

The project supports solid-state NMR methods development and structure determination of wild-type human γS-crystallin in the transparent hydrogel state found in the healthy eye lens, as well as the aggregates formed by UV-light damaged proteins and cataract-related variants. The Martin group is experienced in preparation of crystallin proteins: isotopically labeled samples of the transparent hydrogel of the native crystallin and the aggregates associated with cataract have been prepared. As part of this project, new NMR methodology will be developed to investigate the structural factors related to γS-crystallin stability and solubility. Differential isotope labeling of peptide binders and variant crystallins will be used to identify specific residues involved in altered intermolecular interactions, followed by full structure determination of cataract aggregates. Extensive use will be made of deuterated samples and deuterium NMR in the context of multidimensional NMR experiments.

Candidates must have (or be about to earn) a Ph.D. in Chemistry, Physics, or a related discipline, and have experience solving protein structures using MAS NMR. Previous experience with pulse sequence development is desirable but not required.

Please apply online at https://recruit.ap.uci.edu/apply/JPF05254 with a cover letter that also describes your immediate and long-term research goals, a curriculum vitae including publications list, and names for three letters of reference (please do not solicit letters). Review of applications will begin on Oct 1, 2019 and will continue until the position is filled.

The University of California, Irvine is an Equal Opportunity/Affirmative Action Employer advancing inclusive excellence. All qualified applicants will receive consideration for employment without regard to race, color, religion, sex, sexual orientation, gender identity, national origin, disability, age, protected veteran status, or other protected categories covered by the UC nondiscrimination policy.

Rachel W. Martin

Professor of Chemistry

and Molecular Biology & Biochemistry

University of California, Irvine




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