Erica P. Vogel
- Courses5
- Reviews13
- School: DePaul University
- Campus:
- Department: Chemistry
- Email address: Join to see
- Phone: Join to see
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Location:
2400 N Sheffield Ave
Chicago, IL - 60614 - Dates at DePaul University: October 2015 - April 2016
- Office Hours: Join to see
Biography
DePaul University - Chemistry
Science | Fashion | Philanthropy
Apparel & Fashion
Erica
Vogel, Ph.D.
Raleigh-Durham, North Carolina Area
Highly motivated and outgoing PhD physical chemist and quantitative biologist with an interest in interfacing between science and the general population.
Contact:
erica.paige.vogel@gmail.com
Experience
Be Like Missy
Owner
Small boutique focusing on handmade jewelry and leather goods.
North Carolina State University
Postdoc
I used a combination of Oriented Sample (OS) and Magic Angle Spinning (MAS) solid-state NMR to investigate the structures of membrane proteins in lipid environments.
Responsibilities included:
Lab maintenance and inventory
Grant budgeting
Train and mentor graduate students in biochemistry methodology
Present research at an international school for Biomolecular Solid-State NMR
NMR maintenance and trouble-shootingDePaul University
Teaching Assistant Professor of Chemistry
Erica worked at DePaul University as a Teaching Assistant Professor of Chemistry
Meredith College
Assistant Professor of Chemistry
Courses taught:
General Chemistry lecture and lab
Physical Chemistry lecture and lab (Thermo and Quantum)
Advanced Inorganic Chemistry lecture
Chemistry Senior Seminar
Other commitments:
Think Strong - Active Member of Meredith College's advisory committee on critical thinking. Focus on critical thinking infusion across the disciplines and creating a dialogue for critical thinking on campus.
Student Planning Pilot committee member - worked with student advisees to incorporate new software into the advising process.
Research mentor to six students in areas of green chemistry, bio plastic synthesis, chemical education.
Academic advisor to 13 freshmen with majors ranging from Environmental Sustainability to Business.LuLaRoe
Trainer
Erica worked at LuLaRoe as a Trainer
Education
Grand Valley State University
Bachelor of Arts
Chemistry / Professional Emphasis
Michigan State University
PhD
Biophysical Chemistry and Quantitative Biology
West Ottawa High School
High School Diploma
Publications
Quantitation of Recombinant Protein in Whole Cells and Cell Extracts via Solid-State NMR Spectroscopy
Biochemistry
Recombinant proteins (RPs) are commonly expressed in bacteria followed by solubilization and chromatography. Purified RP yield can be diminished by losses at any step with very different changes in methods that can improve the yield. Time and labor can therefore be saved by first identifying the specific reason for the low yield. This study describes a new solid-state nuclear magnetic resonance approach to RP quantitation in whole cells or cell extracts without solubilization or purification. The method is straightforward and inexpensive and requires only ∼50 mL culture and a low-field spectrometer.
Quantitation of Recombinant Protein in Whole Cells and Cell Extracts via Solid-State NMR Spectroscopy
Biochemistry
Recombinant proteins (RPs) are commonly expressed in bacteria followed by solubilization and chromatography. Purified RP yield can be diminished by losses at any step with very different changes in methods that can improve the yield. Time and labor can therefore be saved by first identifying the specific reason for the low yield. This study describes a new solid-state nuclear magnetic resonance approach to RP quantitation in whole cells or cell extracts without solubilization or purification. The method is straightforward and inexpensive and requires only ∼50 mL culture and a low-field spectrometer.
Solid-State Nuclear Magnetic Resonance (NMR) Spectroscopy of Human Immunodeficiency Virus gp41 Protein That Includes the Fusion Peptide: NMR Detection of Recombinant Fgp41 in Inclusion Bodies in Whole Bacterial Cells and Structural Characterization ...
Biochemistry
Human immunodeficiency virus (HIV) infection of a host cell begins with fusion of the HIV and host cell membranes and is mediated by the gp41 protein, a single-pass integral membrane protein of HIV. The 175 N-terminal residues make up the ectodomain that lies outside the virus. This work describes the production and characterization of an ectodomain construct containing the 154 N-terminal gp41 residues, including the fusion peptide (FP) that binds to target cell membranes. The Fgp41 sequence was derived from one of the African clade A strains of HIV-1 that have been less studied than European/North American clade B strains. Fgp41 expression at a level of 100 mg/L of culture was evidenced by an approach that included amino acid type 13CO and 15N labeling of recombinant protein and solid-state NMR (SSNMR) spectroscopy of lyophilized whole cells. The approach did not require any protein solubilization or purification and may be a general approach for detection of recombinant protein. The purified Fgp41 yield was 5 mg/L of culture. SSNMR spectra of membrane-associated Fgp41 showed high helicity for the residues C-terminal of the FP. This was consistent with a “six-helix bundle” (SHB) structure that is the final gp41 state during membrane fusion. This observation and negligible Fgp41-induced vesicle fusion supported a function for SHB gp41 of membrane stabilization and fusion arrest. SSNMR spectra of residues in the membrane-associated FP provided evidence of a mixture of molecular populations with either helical or β-sheet FP conformation. These and earlier SSNMR data strongly support the existence of these populations in the SHB state of membrane-associated gp41.
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