Zain Bukhari

Postdoctoral Research Scholar,

Biodesign Center for Mechanisms of Evolution

[email protected]

Arizona State University School of Life Sciences P.O. Box 874601 Tempe, AZ 85287-4601
Mail code: 7701

Campus: Tempe
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Long Bio

As a Scientist with diverse experience in analytical methods, statistical visualization, and experimental design, Bukhari has a proven track record of optimizing research processes and mentoring teams for impactful outcomes. Skilled in computational pipelines, teaching, protein purification, and molecular cloning, he excels in conducting complex experiments and leading research initiatives. With a background in maintaining state-of-the-art laboratory equipment, supervising professional development for colleagues, and developing a variety of biochemical tests, Bukhari is adept at fostering innovative environments that enable scientific discovery.

Education

2024: Molecular and Cellular Biology (Ph.D.), School of Life Sciences, Arizona State University - Tempe Campus, AZ

2018: Nanoscience (P.S.M.), Department of Physics, Arizona State University - Tempe Campus, AZ

2017: Biochemistry (B.S.), Barrett College, AZ

2013: High School Diploma, Gilbert Classical Academy, AZ

Research Website URL

https://www.thefraschlab.org/

Google Scholar URL

https://scholar.google.com/citations?user=lMZkSl0AAAAJ

Research Interests

For over five years, Bukhari worked with ASU's Human Anatomy & Physiology program in the School of Life Sciences, leading the team of BIO 201 TAs (in Spring 2018 / Spring 2019) and BIO 202 TAs (in Spring 2018 / Fall 2019) at the Tempe campus. In addition, Bukhari worked with ASU Online and New Media Studios at EdPlus to produce over 145 video lectures for the university's fully online Anatomy & Physiology courses.

Today, Bukhari is involved with Dr. Wayne Frasch's biophysical/biochemical research on ATP Synthases, namely the F-type and V-type.

Research Group

Wayne Frasch’s lab has developed new assays to examine the rotation of single molecules of molecular motor proteins under a microscope. The lab focuses on the Fo and F1-ATPase rotary motors that comprise the F-type ATP synthase. This protein complex synthesizes the majority of ATP in almost all living organisms, which provides the energy for many cellular processes.

The research group also creates nano-scale devices by assembling molecules of DNA and proteins in novel ways that can carry out specific tasks. These include the incorporation of the F1-ATPase molecular motor into devices that detect single molecules of toxins, drugs or DNA profiles of interest that can provide an early indication of infection or disease. Other nano-devices use the assembly of DNA molecules to make computations, such as precise calculation of telomere lengths to quantify cellular aging.

Publications

Available on Google Scholar.

Presentations

The F1-ATPase Rotary Mechanism; Seminar. School of Life Sciences Molecular and Cellular Biology Colloquium, Arizona State University; 2021
Characterization of the Role of Rab5a in Causing Cancer Cell Invasiveness via an in vitro Model; Proposal. School of Life Sciences Molecular and Cellular Biology Comprehensive Exams Defense, Arizona State University; 2021
Angular Velocity and Dwell Analyses of the F1-ATPase Molecular Motor; Preview Presentation. Gordon Research Conference on Bioenergetics, Andover, NH; 2019; https://www.grc.org/bioenergetics-conference/2019/
Ditto; Poster. Gordon Reserach Conference on Bioenergetics, Andover, NH; 2019
Dwell Analyses of the F1-ATPase Molecular Motor; Seminar. School of Life Sciences Molecular and Cellular Biology Colloquium, Arizona State University; 2019; https://biodesign.asu.edu/news/dwell-analyses-f1-atpase-molecular-motor…
Torsion Spring Contributions to the F1-ATPase Molecular Motor Mechanism; Supervised Applied Project Defense. Department of Physics, Arizona State University; 2018; https://nanoscience.asu.edu/students/zain-bukhari
Ditto; Poster. Department of Physics Nanoscience Capstone Conference, Arizona State University; 2018
Dependence of the angular velocity of rotation on rotational position at which ATP-binding occurs at the empty catalytic site of the F1-ATPase molecular motor; Thesis Defense. Barrett, the Honors College, Arizona State University; 2017; http://hdl.handle.net/2286/R.I.42248