Org Marketing Statement
All over the world, Pfizer colleagues are working together to positively impact health for everyone, everywhere. Each position at Pfizer touches and contributes to the success of our business and our world. That’s why, as one of the global leaders in the biopharmaceutical industry, Pfizer is committed to seeking out inspired new talent who share our core values and mission of making the world a healthier place.
Role Description
The successful candidate will be responsible for developing robust methods for the characterization of protein higher order structure using mass spectrometric methods, including H/D exchange, radical protein footprinting, and ion mobility. The position is located in the Mass Spectrometry and Biophysical Characterization group in the Biotherapeutics Pharmaceutical Sciences department, which is responsible for the structural characterization of Pfizer’s Biotherapeutics clinical candidates. The goal for the candidate is to develop mass spectrometry-based higher order structure methods for application to biotherapeutic proteins in clinical development. The candidate will be expected to evaluate the methods in comparison to well-established biophysical methods for higher order structure characterization. The candidate will be expected to become established as an expert in the field of mass spectrometry-based methods for higher order structure characterization. The desired outcome is the publication of results in peer-reviewed journals and presentations at scientific conferences. The candidate will work within the Mass Spectrometry and Biophysical Characterization group within the Biotherapeutics Pharmaceutical Sciences department, and collaborate with allied research units and partner lines to develop and implement characterization methods.
Responsibilities
The qualified candidate will be responsible for developing and applying mass spectrometric methods of analysis to the characterization of higher order structure of biotherapeutic proteins, including H/D exchange, radical protein footprinting, and ion mobility MS. Comparison of results to current/standard biophysical methods for the characterization of protein higher order structure is expected. The qualified candidate will develop methods that can be applied to multiple programs to positively impact regulatory submissions and product knowledge. The candidate will be expected to generate data and author manuscripts for publication in peer-reviewed journals and to present at scientific conferences.
Qualifications
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Ph. D. in Chemistry, Biochemistry, or related field, with 0-2 years postdoctoral experience is required.
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A strong background in the use of mass spectrometry for the characterization of protein structure and the determination of post-translational modifications and protein degradation pathways is required.
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Extensive experience in protein chemistry as applied to the characterization of biotherapeutic proteins, including enzymatic digestion, chromatographic separations, conjugation, and detection is required.
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Specific experience with H/D exchange and/or ion mobility mass spectrometry is highly desirable, although candidates without direct experience in these areas will be considered.
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A working knowledge of orthogonal bioanalytical methods such as circular dichroism spectroscopy and/or fluorescence spectroscopy is also desirable.
- Strong written and verbal communication skills are expected, and a demonstrated history of publications in peer-reviewed journals and presentations at national conferences is desired.
Pfizer is committed to equal opportunity in the terms and conditions of employment for all employees and job applicants without regard to race, color, religion, sex, sexual orientation, age, gender identity or gender expression, national origin, disability or veteran status. Pfizer also complies with all applicable national, state and local laws governing nondiscrimination in employment as well as employment eligibility verification requirements of the Immigration and Nationality Act. All applicants must have authorization to work for Pfizer in the U.S. In certain circumstances it may be advantageous to Pfizer to support the application(s) for temporary visa classification and/or sponsor applications for permanent residence so that a foreign national colleague can accept or remain in a work assignment in the U. S. For certain classes of temporary visas, the resulting work authorization may be specific to Pfizer and the specific job and/or work site. Pfizer may at its business discretion decide to or refrain from obtaining, maintaining and/or extending the temporary visa status and/or sponsoring a colleague for permanent residency and /or employment eligibility, considering factors such as availability of qualified U.S. workers and the colleague's long-term prospects for securing lawful permanent residence, among other reasons. Employment applicants requiring immigration sponsorship must disclose, when initial application for employment is made, whether or not they are legally authorized to work for Pfizer in the U.S. and, if so, whether that authorization permits them to work in the job they seek. In no case should Pfizer's support of a colleague's temporary visa application or sponsorship of a colleague for permanent residence be construed to guarantee success of that application or amend or otherwise invalidate the "at-will" employment relationship between the colleague and Pfizer.
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A working knowledge of orthogonal bioanalytical methods such as circular dichroism spectroscopy and/or fluorescence spectroscopy is also desirable.
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Specific experience with H/D exchange and/or ion mobility mass spectrometry is highly desirable, although candidates without direct experience in these areas will be considered.
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Extensive experience in protein chemistry as applied to the characterization of biotherapeutic proteins, including enzymatic digestion, chromatographic separations, conjugation, and detection is required.
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A strong background in the use of mass spectrometry for the characterization of protein structure and the determination of post-translational modifications and protein degradation pathways is required.
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